IGF-1 Information Here!

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  1. IGF-1 Information Here!

    R3(long) IGF-1

    1: Type- IGF-1 Long R3 (Anything else is not as effective, and if the person providing it for you doesn't know anything about it, you are asking for trouble.)
    2. Storage- the most popular (and most effective) way to store, transport, preserve IGF is by suspending it in sterile BA in a sterile vial.
    This will keep your IGF 99% potent for many months at a time in just about ANY indoor storage, I.E.-closet, drawer, etc. (Take it from me, I stored mine because I wasn't ready to use it for about 6 months in my closet... I had fears about its potency, then I started my first week, and BAM I practically cleaned out the fridge.
    3. Use- Usage should not exceed 4-5 weeks, and an OFF period should be about the same. Daily dosages work best (split up into 2 seems to make little difference in the Long R3 version) Most people see results at about 40mcg/day, some use as low as 30mcg/day, and some folks even use 80-100mcg. I SUGGEST to ALL first time users no matter what level, to start at about 40-50mcg/day.
    4. Administration- I believe in IM injections over sub q, but either seems to be effective. I like IM better because IM using a slin pin is probably the least painful thing one could imagine, even at two times per day. Also, sub Q shots that contain BA, even diluted BA, can leave little nodules that you may not want to feel on your stomach.
    5. Mixing- Most IGF comes suspended in BA. Hopefully it is @ 500mcg/ml or even 333mcg/ml (that would be at 2ml/mg and 3ml/mg respectively) Draw out your desired amount and back load a slin pin. Add enough Bacteriostatic Water to fill the U100 syringe completely.
    Some inject immediately before training, while others choose to do 2 shots spread throughout the day... THEY BOTH WORK WELL. Try both; see which method makes your muscles pop out of your skin.
    6. Add plenty of protein, and don’t shy away from carbs immediately after training. I used up to 100g of carbs after training, and my body fat went down, all without cardio.



    IGF stands for insulin-like growth factor. It is a natural substance that is produced in the human body and is at its highest natural levels during puberty. During puberty IGF is the most responsible for the natural muscle growth that occurs during these few years. There are many different things that IGF does in the human body; I will only mention the points that would be important for physical enhancement. Among the effects the most positive are increased amino acid transport to cells, increased glucose transport, increased protein synthesis, decreased protein degradation, and increased RNA synthesis.

    When IGF is active it behaves differently in different types of tissues. In muscle cells proteins and associated cell components are stimulated. Protein synthesis is increased along with amino acid absorption. As a source of energy, IGF mobilizes fat for use as energy in adipose tissue. In lean tissue,

    IGF prevents insulin from transporting glucose across cell membranes. As a result the cells have to switch to burning off fat as a source of energy.

    IGF also mimic's insulin in the human body. It makes muscles more sensitive to insulin's effects, so if you are a person that currently uses insulin you can lower your dosage by a decent margin to achieve the same effects, and as mentioned IGF will keep the insulin from making you fat.

    Perhaps the most interesting and potent effect IGF has on the human body is its ability to cause hyperplasia, which is an actual splitting of cells. Hypertrophy is what occurs during weight training and steroid use, it is simply an increase in the size of muscle cells. See, after puberty you have a set number of muscle cells, and all you are able to do is increase the size of these muscle cells, you don't actually gain more. But, with IGF use you are able to cause this hyperplasia which actually increases the number of muscle cells present in the tissue, and through weight training and steroid usage you are able to mature these new cells, in other words make them grow and become stronger. So in a way IGF can actually change your genetic capabilities in terms of muscle tissue and cell count. IGF proliferates and differentiates the number of types of cells present. At a genetic level it has the potential to alter an individuals capacity to build superior muscle density and size.

    There is a lot of talk about the similarity between IGF and growth hormone. The most often asked question is simply which is more effective. GH doesn't directly cause your muscles to grow, it works very indirectly by increasing protein synthesis capabilities, increasing the amount of insulin a person can use effectively, and increasing the amount of anabolic steroids a person can use effectively. GH also indirectly causes muscle growth by stimulating the release of IGF when it (the GH) is destroyed in the human body. So one way you could look at it as GH being a precursor to IGF. So to put it simple IGF is more effective at directly causing muscle growth and density increases. IGF is also much more cost effective.

    IGF can also be effectively used by itself and gains will still be easily noticeable. With growth hormone you need to use high amounts of anabolics and often insulin to see any gains at all, this is not the case with IGF. IGF can be used by itself and is often used by bodybuilders who bridge between cycles, during this bridge is a good time to use IGF since it has no effect on natural testosterone production so it will therefore allow you to return to normal in terms of hormone levels. A stack of IGF, PGF2a, HCG, and clomid would be a good bridge stack and would allow your body to return to normal and still allow you to retain and make new gains.

    IGF is a research drug, it hasn't been approved by the FDA for use as a pharmaceutical and it is currently being researched for nerve tissue repair, possible burn victims, and also as a possible aid in muscle wasting for AIDS patients. There are many different analogs of IGF available, instead of mentioning them all, I will simply mention the two most common and the most effective. Regular recombinant IGF is one of the two, it is also the more expensive and the least effective. Regular IGF only has a half-life of about 10-20 minutes in the human body and is quickly destroyed, it can be combined with certain binding proteins to extend the half-life, but it is not a very simple procedure and there is a more effective and less expensive version available. The most effective form of IGF is Long R3 IGF-1, it has been chemically altered and has had amino acid changes which cause it to avoid binding to proteins in the human body and allow it to have a much longer half life, around 20-30 hours. "Long R3 IGF-1 is an 83 amino acid analog of IGF-1 comprising the complete human IGF-1 sequence with the substition of an Arg(R) for the Glu(E) at position three, hence R3, and a 13 amino acid extension peptide at the N terminus. This analog of IGF-1 has been produced with the purpose of increasing the biological activity of the IGF peptide."

    "Long R3 IGF-1 is signifacantly more potent than IGF-1. The enhanced potency is due to the decreased binding of Long R3 IGF-1 to all known IGF binding proteins. These binding proteins normally inhibit the biological actions of IGF's."

    It is also not as expensive since a media grade version is available which is sufficient for bodybuilding use. There is also a receptor grade available but it is VERY expensive and the only noticeable difference between the two would only be able to be noticed in a laboratory setting. The price on the black market for Long R3 IGF-1 can be seen anywhere from $300-$500 per milligram depending on the source, be wary of black market ******s of any IGF since it is a VERY difficult item to obtain. As mentioned IGF is a research product and is only available from a few laboratories in the world and is only available to research companies and biotechnology institutions. For the rest of this article when I say IGF I am now referring to Long R3 IGF-1 for simplicity sake.

    Any form of IGF is ONLY supplied in a lyphosized form, which means a dry powder state. NEVER PUCHASE PRE-DILUTED LIQUID IGF!!!! There is no such product made anywhere in the world and even if there were real IGF ever present in the vial it would all be dead by the time you receive it. IGF is a very delicate peptide and must be diluted by yourself, where you have access to a refrigerator and freezer. There has also been a lot of talk by certain sources claiming to have IGF made by the Eli Lilly company, to clear things up Lilly is a pharmaceutical company and as stated IGF is a research drug and has not yet been approved, Lilly does not and never has manufactured research drugs for retail sale.

    The dilutents you will need for the IGF are a weak concentration of hydrochloric acid and a sterile buffer(sterile water or bacteriostatic water) the procedure for diluting the IGF is not very difficult, the dilutents can be obtained from most local chemical suppliers and a good source of IGF would also be able to supply the necessary dilutents.

    The most effective length for a cycle of IGF is 50 days on and 20-40 days off. The most controversy surrounding Long R3 IGF-1 is the effective dosage. The most used dosages range between 20mcg/day to 120+mcg/day. IGF is only available by the milligram, one mg will give you a 50 day cycle at 20mcg/day, 2mg will give you a 50 day cycle at 40mcg/day, 3mg will give you a 50 day cycle at 60mcg/day, 4mg will give you a 50 day cycle at 80mcg/day and so on. The dosage issue mainly revolves around how much money you have to spend, plenty of people use the minimum dosage of 20mcg/day and are happy with the results, and in fact several top bodybuilders use the 20mcg/day dosage and are pleased with the results. IGF is most effective when administered subcutaneously and injected once or twice daily at your current dosage. The best time for injections is either in the morning and/or immediately after weight training.

    Another frequently asked question of IGF refers to the real world results, in terms of pure weight gain don't expect to gain 5 lbs. a week like you may off of anadrol or a similar steroid. The only weight you will gain from IGF use is pure lean muscle tissue, with steroids most of the weight gained is water weight. With an effective dosage you can expect to gain 1-2 lbs of new lean muscle tissue every 2-3 weeks and these effects can be increased with the use of testosterone, anabolic steroids, and insulin use. Increased vascularity is also very common, people report seeing veins appear where they never have before. And yet another effect reported is the ability to stay lean while bulking with heavy dosages of steroids and TONS of food while on an IGF cycle, this is perhaps the most pleasing effect. Increased pumps are also noticeable almost immediately, the pumps can almost become painful, pumps are even noticeable when doing cardio.

    Overall, IGF is a very exciting drug due to its ability to alter ones genetic capabilities. If you can find a trustworthy source and you use it correctly it can be a VERY useful tool in your bodybuilding drug arsenal.


    All these are taken from other posts:

    The conversion rate of GH is more like 1 iu gh = 4-6 mcg of igf-1.

    If this is true (and let's pick 5mcg for an avg), 30mcg of igf = 6ius of GH. I've done enough GH to comment that it may be slightly better than this. The only bad thing is that it stops working in 4-6 weeks. Then you have to take the same time off as you were on before starting again. It has something to do with how the IGF was modified to produce the "long" version and your body eventually figures it out.


    Comment from a user:

    One more thought on IGF-1 Long-R. It cutting properties are truly amazing but I think it would be a waste of ammo to use it in a cutter. I think adding it to the last weeks of a bulking cycle is the way to best utilize it. In another post I've read, someone said it helps to solidify gains. Well if you are like me, the lbs at the end of a bulking cycle are the hardest to come by. Also the end is where I put on the most fat.

    I'm coming to the end of a bulk cycle this Sat. I started IGF in week 5 (of an 8 week cycle). I originally posted I added 750 calories a day. Well going back to check my training log I was a little off. I added 600 calories in week 5 (as soon as I started to lose weight) and another 300 in week 6. I weighed in at the beginning of week 8 and I dropped 3 more lbs. I'll weigh in again Sat for the final tally. At the end of week 4 I had put 1 1/4 inches on my waist. As of the beginning of week 8 the number dropped by 3/4 of an inch, down to a 1/2 inch waist gain. Strength has increased each week of this cycle. Now before you read too much into all these figures I was off for 2 1/2 months with the achilles injury. So alot of this can be attributed to rebound. I did set new PB's on delts and are very close on other bodyparts. I'm 44 yrs old too, so that plays into recovery abilities (not for the good).

    I do have a 25 yr old friend who uses it as a bridge between cycles. This guy has a hard time keeping gains. He does follow all the post-cycle regime to a "T". It has allowed him to keep more post cycle than he has in the past.
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  2. From Basskiller:

    IGF1, also known as somatomedin C, is polypeptide hormone about the same size as insulin. It is produced predominantly in the liver in response to growth hormone (GH) release from the pituitary gland. Many of the growth promoting effects of GH are due to its ability to release IGF1 from the liver. The conversion ratio of GH to IGF1 varies greatly in different individuals but most external sources of GH convert around 4-6mcg of IGF per one I.U. of GH. IGF-1 acts on several different tissues to enhance growth. IGF1 belongs in the 'superfamily' of substances known as 'growth factors,' along with epidermal (skin), transforming; platelet derived fibroblast, nerve, and ciliary neurotrophic growth factors. None of the other factors have any bearing on exoskeletal tissue incidentally however These agents all have in common the ability to stimulate cell division, known as mitogenesis, and cell differentiation. Meaning That In the case of IGF1 which does act on muscle tissue it will initiate the growth of new muscle fibers, and subsequently new receptors for testosterone. Users have unanimously concluded that it enhances cycles of steroids significantly. They also seem to be adamant about its ability to reduce fat and improve vascularity a great deal.

    The IGF1 Hype

    There is a considerable amount of hype surrounding IGF1. Every one is blaming the distended bellies of modern Bodybuilders on it. Also the freaky proportions that old bodybuilders that have been around for years are starting to attain. Anti-aging proponents are touting it as the miracle cure for every thing from Parkinson's disease to Alzheimer's. And the medical community has published numerous articles on it for its ability to cause cancer, diabetes and gigantism. While at the same time performing documented experiments on thousands of patients of muscle wasting diseases. And reporting significant turnabouts in there conditions. So what is a guy to think about IGF1 as far as athletic enhancement is concerned? Well first of all you need to know that most experiments conducted with IGF1 do not list the type of IGF used. I have written Dr. Robert Saline of the Swedish rejuvenation institute on several occasions and we have had in-depth discussions on the subject of IGF1 for physical appearance enhancement. He feels it would be unethical to prescribe IGF1 to a bodybuilder to increase muscle mass simply due to the fact that IGF1 has valid applications in the medical community, (Like I could give a rats ass about "ethical"). He can not argue that it is extremely effective as a promoter of muscle growth far beyond what androgens (steroids) alone can offer. Well fortunately in America IGF1 is not a drug (yet) and the FDA has no control over it as of now. This will change in the very near future however, Im absolutely sure of it.

    How to use IGF1

    Assuming that you have acquired legitimate IGF1 (R3) long chain, That's IGF1 with the binding protein added. You should take dosages ranging from 60mcg up to 120mcg per day in divided doses. One injection in the morning and again at bed time. Never exceed 120mcg in one day. IGF1 can cause serious gastrointestinal problems such as tumors intestinal swelling diarrhea and vomiting. Most IGF1 comes in a concentration of 1000mcg per ML or CC so it makes it easy to measure in an insulin syringe. 10 IU on the syringe is 100mcg. Do the math.

    IGF + Insulin

    If you plan on doing IGF1 with Insulin, listen closely IGF1 is not that expensive, sure you can get away with using less by including insulin in the stack, but IGF1 and Insulin together have a pro-insulin effect on your blood sugar balance. It can enhance the chances of a hypoglycemic episode ten fold. I would recommend against it for any one not ABSOLUTLY comfortable with insulin or IGF1.

    Here is how insulin and IGF1 work together. Igfbp3 is the binding protein, which allows IGF1 to remain active in the system for a long enough period of time to really work its magic. IGF1 by nature has a half-life of less than 10 minutes by its self. The molecule was so small it would escape the blood stream very rapidly. This was the reason IGF1 was so "underground". It took very frequent injections at high dosages to achieve even minimal results. Aside from this reconstituting the compound required a degree in biochemistry. This short acting version was the only IGF1 known until recently IGF1 would have been administered in 100 mcg dosages 4-6 times a day. That is a hell of a lot of IGF1. That explains a lot of the distended bellies. Now with R3 long chain IGF1 and the Binding protein IGFBP3 IGF1 will last up to 6 hours in the system. By binding IGF to the IGFBP3 you make the molecule larger and it gets trapped in the blood stream until the protein is broken down and the IGF molecule escapes. You can further its life by combining Insulin with it, although I here its very risky. Insulin prevents the breakdown of IGFBP3 and leaves the IGF1 molecule roaming free in the blood stream for longer periods of time up to 12 hours as insulin levels return to normal IGFBP3 will begin to break down and the IGF1 will escape from its bound protein IGFBP3 again having a half life of less than 10 minutes.

    Insulin should be taken at the normal dosage it is usually administered at minus 10% about 45 minutes prior to the IGF1 infusion. Again let me remind you this can be deadly if you don't know what you are doing. And of course do not use Insulin for the nighttime injection of IGF1 by taking it in the morning you prolong the IGF1's half life to 12 hours and then take a 6 hour injection, you should be fine. Hell if you want to eat a big bowl of rice and drink another 100g of simple carbs 45 minutes before the bed time IGF1 infusion you could spike insulin for at least a few hours of extended IGF1 activity. If your not going to be using insulin in the stack then go ahead and do the same in the morning.

    What users report

    Users of IGF1 have reported various results but all along the same lines, It does not appear to be dramatically less effective in any one individual (at least not to the best of my knowledge). I have a good friend who had to stop taking IGF1 due to stomach illness that was completely unrelated But he to experienced good gains from it for the 2 weeks he was on it, his dosage was 120mcg per day. One hour after the first injection he went to the gym and immediately told me about the uncontrollable pump he got from just one set.

    That would indicate to me that he was experiencing some form of cell volumization. The general consensus on IGF1 seems to be that its benefits are as fallow:

    Increased Pump Pumps are reported to be so severe that workouts are often cut short due to lack of ability to the muscle through the full range of motion...ouch

    Gains retention is increased if IGF is used in a cycle I am not sure why, but IGF1 seems to make gains on a cycle stick with virtually no post cycle loss. Every bodybuilder I've spoken with seems to think this for some reason. Most of them use drugs like Anadrol or Dianabol with it because of the amount of size attained with these drugs. The usual draw back to these drugs is that in most users there is a post cycle "crash" that occurs, so the reasoning is to toss IGF1 into the stack and grow larger faster with out the post cycle crash blues.

    Reverses testicular atrophy

    Testicles if shrunken will return to "full swing" so to speak even in the middle of a cycle. If not shrunken they will not shrink during the cycle. This may explain partially why gains are kept after the cycle.


    Users report feeling drained and tired all day. This seems to be one of the negative side effects to IGF1, it will make you sleep longer and you will require more sleep at night to feel rested for the morning. This is common with high doses of HGH and exhibited in children, whose IGF1 levels are extraordinarily high. A child needs 4 hours more sleep than an adult on average does. This may be directly or indirectly related to IGF1 levels.


    An almost arthritic feeling is commonly associated with high levels of HGH, well IGF1 has the exact same property. IGF1 will cause your hands, fingers and knuckles to ache this is one way you can be sure you got real IGF1.

    IGF-1's Side effects

    Every thing has a down side. To bake a cake ya gotta brake an egg. IGF1 is no exception. The drug used in larger quantity around the 100mcg+ range will cause headaches, occasional nausea and can contribute to low blood sugar or hypoglycemia in some users. Although I have never heard of this first hand I'm sure its true.

    IGF1 will attach its self to the lining of the intestine and cause atrophy of the gut. Every thing IGF1 touches will grow and you have a lot of receptors on the lining of the large intestine and inner wall of the abdominal well. This is what causes the GH gut look. You can easily avoid this by limiting your dosages and cycle lengths. IGF1 cycles should be kept to 4-6 weeks with 4-6 weeks off in-between. IGF-1 is considerably more powerful than HGH and you need to think of it along those lines as far as dosing goes. We all know what to much HGH can do over prolonged periods of usage. The Neanderthal look is definitely not going to win any shows this year. I would recommend 80 mcg a day for 4 weeks at a time you should get good results from that for a while. I don't know if you will need to up the dosage at any point, but I would think in the case of IGF1 it wouldn't matter. If 80mcg doesn't do it for ya, then bump it up to 100 You should definitely feel it at this point If not suspect the IGF1 as being fake. Beyond 120 mcg per day your asking for trouble, This compound demands as much respect as its sister amino Insulin.

    Clinical Facts about IGF-1

    IGF-1 is a polypeptide of 70 amino acids (7650 daltons), and is one of a number of related insulin-like growth factors present in the circulation. The molecule shows approximately 50% sequence homology with proinsulin and has a number of biological activities similar to insulin. IGF-1 is a mediator of longitudinal growth in humans or how tall you are capable of becoming. Serum IGF-1 concentrations are altered by age, nutritional status, body composition, and growth hormone secretion. A single basal IGF-1 level is useful in the assessment of short stature in children and in nutritional support studies of acutely ill patients. For the diagnosis of acromegaly, a single IGF-1 concentration is more reliable than a random hGH measurement (Oppizi, et al., 1986). IGF-1 can be used for the assessment of disease activity in acromegaly (Barkan, et al., 198.

    Almost all (>95%) of serum IGF-1 circulates bound to specific IGF binding proteins (IGFBPs), of which six classes (IGFBPs 1-6) have been identified (Rudd, 1991). BP3 is thought to be the major binding protein
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  3. Nice and very informative.
    Thanks Bobo.

  4. Do localized (site specific) injections provide any benefit or is the abdomen the only spot I should hit?

  5. Some say yes but scientifically its not the same. Localized IGF-1 (mechano-growth factor) is not the same thing as the IGF-1 in Long R3 so it shouldn't cause localized growth. The effects should stem from an increase in systemic IGF-1 that is resistant to IGFBP3.
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  6. Quote Originally Posted by Bobo
    Some say yes but scientifically its not the same. Localized IGF-1 (mechano-growth factor) is not the same thing as the IGF-1 in Long R3 so it shouldn't cause localized growth. The effects should stem from an increase in systemic IGF-1 that is resistant to IGFBP3.
    Localized IGF-1 (that specific to skeletal muscle) is IGF-1Ea. IGF-1Eb (MGF) is also specific to skeletal muscle, but is expressed only in response to stretch or electrostimulation. LR3 injected into muscles will have the same type of hyperplasia effects that are induced by IGF-1Ea. A recent paper expresed the hepatic form of IGF-1 in mouse muscles and showed a significant increase in cross sectional area and a significantincrease in recruitment of satellite cells into mature myocytes. Site specific effects are not only possible but common. IM is the most sensible way to go, being that you'd like to introduce the greatest concentration of IGF-1 to the area with the greatest concentration of IGF receptors (that being the muscle just worked).

  7. Can you please post that paper because of all the studies I have seen (mostly over at CEM) do not equate hepatic IGF-1 to increased MGF at all. I think an overall increase in hepatic IGF-1 can cause hyperplasia and increase MGF in all muscle groups but not in specifically injected muscle groups.
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  8. You also to to take into account the mouse studies especially in this case are very inconclusive because in different animals it has different effects. It it anabolic in rats but catabolic in pigs (because it lowers GH, IGF-1 and insulin). THis effect is not seen in rats so the effects in humans are unknown.
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  9. Was this the paper? Becuase they used mIGF-1 that is the isoform found in skeletal and cardiac muscle and would not represent Long R3 IGF-1

    "The Igf-1 isoform used here (referred to as mIgf-1) is normally synthesized in skeletal and cardiac muscle13. We generated transgenic mice with a rat mIgf-1 cDNA driven by skeletal muscle-specific regulatory elements from the rat myosin light chain (MLC)-1/3 locus."

    Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle

    Antonio Musarň1, 2, Karl McCullagh1, Angelika
    Paul1, Leslie Houghton1, Gabriella Dobrowolny2, Mario Molinaro2, Elisabeth R. Barton3, H. L Sweeney3 & Nadia Rosenthal1

    If thats not the study, then ignore that.
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  10. Quote Originally Posted by Bobo
    Was this the paper? Becuase they used mIGF-1 that is the isoform found in skeletal and cardiac muscle and would not represent Long R3 IGF-1

    "The Igf-1 isoform used here (referred to as mIgf-1) is normally synthesized in skeletal and cardiac muscle13. We generated transgenic mice with a rat mIgf-1 cDNA driven by skeletal muscle-specific regulatory elements from the rat myosin light chain (MLC)-1/3 locus."

    Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle

    Antonio Musarň1, 2, Karl McCullagh1, Angelika
    Paul1, Leslie Houghton1, Gabriella Dobrowolny2, Mario Molinaro2, Elisabeth R. Barton3, H. L Sweeney3 & Nadia Rosenthal1

    If thats not the study, then ignore that.
    Actually a more recent paper by some of the same people. I have many relevant IGF-1 papers, if you want me to post them. I don't want to eat up bandwidth if it's not ok. What I was referring to was that the hepatic isoform of IGF-1 was expressed in rat muscle and caused the hyperplasia effects that had been only associated with the muscle-specific isoforms of IGF-1 before. Also, the hepatic-derived IGF-1 isn't actually causing the upregulation of muscle-specific isoforms within skeletal muscle, but rather GH itself binds GH receptors on skeletal muscle, which causes upregulation of the IGF-1Ea isoform in muscle.

    I'd gladly post some references w/abstracts if you'd like. Lots of good stuff. The most recent, 3-2004 paper is most relevant to us, as it incorporates resistance training into the equation.

  11. Post EVERYTHING!!!


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  12. Take from it what you will.......
    I also have several GH papers, but that's for a different day.

    J Appl Physiol. 2004 Mar;96(3):1097-104. Related Articles, Links

    Viral expression of insulin-like growth factor-I enhances muscle hypertrophy in resistance-trained rats.

    Lee S, Barton ER, Sweeney HL, Farrar RP.

    Department of Kinesiology, University of Texas, Austin 78712, USA.

    Muscle hypertrophy is the product of increased drive through protein synthetic pathways and the incorporation of newly divided satellite cells. Gains in muscle mass and strength can be achieved through exercise regimens that include resistance training. Increased insulin-like growth factor-I (IGF-I) can also promote hypertrophy through increased protein synthesis and satellite cell proliferation. However, it is not known whether the combined effect of IGF-I and resistance training results in an additive hypertrophic response. Therefore, rats in which viral administration of IGF-I was directed to one limb were subjected to ladder climbing to test the interaction of each intervention on muscle mass and strength. After 8 wk of resistance training, a 23.3% increase in muscle mass and a 14.4% increase in peak tetanic tension (P(o)) were observed in the flexor hallucis longus (FHL). Viral expression of IGF-I without resistance training produced a 14.8% increase in mass and a 16.6% increase in P(o) in the FHL. The combined interventions produced a 31.8% increase in muscle mass and a 28.3% increase in P(o) in the FHL. Therefore, the combination of resistance training and overexpression of IGF-I induced greater hypertrophy than either treatment alone. The effect of increased IGF-I expression on the loss of muscle mass associated with detraining was also addressed. FHL muscles treated with IGF-I lost only 4.8% after detraining, whereas the untreated FHL lost 8.3% muscle mass. These results suggest that a combination of resistance training and overexpression of IGF-I could be an effective measure for attenuating the loss of training-induced adaptations.

    FASEB J. 2003 Jan;17(1):59-60. Related Articles, Links

    Persistent IGF-I overexpression in skeletal muscle transiently enhances DNA accretion and growth.

    Fiorotto ML, Schwartz RJ, Delaughter MC

    Adult transgenic mice with muscle-specific overexpression of insulin-like growth factor (IGF)-I have enlarged skeletal muscles. In this study, we; 1) characterized the development of muscle hypertrophy with respect to fiber type, age, and sex; 2) determined the primary anabolic process responsible for development of hypertrophy; and 3) identified secondary effects of muscle hypertrophy on body composition. Transgene expression increased with age and was present only in fibers expressing type IIB fast myosin heavy chain. Muscle masses were greater by 5 wk of age, and by 10 wk of age the differences were maximal despite continued transgene expression. Total DNA and RNA contents of the gastrocnemius muscle were greater for transgenic mice than for nontransgenic littermates. The differences were maximal by 5 wk of age and preceded the increase in protein mass. The accelerated protein deposition ceased when the protein/DNA ratio attained the same value as in nontransgenic controls. Despite localization of IGF-I expression to muscle without changes in plasma IGF-I concentrations, genotype also modified the normal age and sex effects on fat deposition and organ growth. Thus, enhanced DNA accretion by IGF-I was primarily responsible for stimulating muscle growth. In turn, secondary effects on body composition were incurred that likely reflect the impact of muscle mass on whole body metabolism.

    J Physiol. 2004 Feb 15;555(Pt 1):231-40. Epub 2003 Oct 17. Related Articles, Links

    The effect of recombinant human growth hormone and resistance training on IGF-I mRNA expression in the muscles of elderly men.

    Hameed M, Lange KH, Andersen JL, Schjerling P, Kjaer M, Harridge SD, Goldspink G.

    Department of Surgery, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, UK. [email protected]

    The expression of two isoforms of insulin-like growth factor-I (IGF-I): mechano growth factor (MGF) and IGF-IEa were studied in muscle in response to growth hormone (GH) administration with and without resistance training in healthy elderly men. A third isoform, IGF-IEb was also investigated in response to resistance training only. The subjects (age 74 +/- 1 years, mean +/- S.E.M) were assigned to either resistance training with placebo, resistance training combined with GH administration or GH administration alone. Real-time quantitative RT-PCR was used to determine mRNA levels in biopsies from the vastus lateralis muscle at baseline, after 5 and 12 weeks in the three groups. GH administration did not change MGF mRNA at 5 weeks, but significantly increased IGF-IEa mRNA (237%). After 12 weeks, MGF mRNA was significantly increased (80%) compared to baseline. Five weeks of resistance training significantly increased the mRNA expression of MGF (163%), IGF-IEa (68%) and IGF-IEb (75%). No further changes were observed after 12 weeks. However, after 5 weeks of training combined with GH treatment, MGF mRNA increased significantly (456%) and IGF-IEa mRNA by (167%). No further significant changes were noted at 12 weeks. The data suggest that when mechanical loading in the form of resistance training is combined with GH, MGF mRNA levels are enhanced. This may reflect an overall up-regulation of transcription of the IGF-I gene prior to splicing.

    J Physiol. 2003 Feb 15;547(Pt 1):247-54. Epub 2002 Dec 20. Related Articles, Links

    Comment in:
    J Physiol. 2003 Feb 15;547(Pt 1):2.

    Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise.

    Hameed M, Orrell RW, Cobbold M, Goldspink G, Harridge SD.

    Department of Physiology, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, UK.

    The mRNA expression of two splice variants of the insulin-like growth factor-I (IGF-I) gene, IGF-IEa and mechano growth factor (MGF), were studied in human skeletal muscle. Subjects (eight young, aged 25-36 years, and seven elderly, aged 70-82 years) completed 10 sets of six repetitions of single legged knee extensor exercise at 80 % of their one repetition maximum. Muscle biopsy samples were obtained from the quadriceps muscle of both the control and exercised legs 2.5 h after completion of the exercise bout. Expression levels of the IGF-I mRNA transcripts were determined using real-time quantitative RT-PCR with specific primers. The resting levels of MGF were significantly (approximately 100-fold) lower than those of the IGF-IEa isoform. No difference was observed between the resting levels of the two isoforms between the two subject groups. High resistance exercise resulted in a significant increase in MGF mRNA in the young, but not in the elderly subjects. No changes in IGF-IEa mRNA levels were observed as a result of exercise in either group. The mRNA levels of the transcription factor MyoD were greater at rest in the older subjects (P < 0.05), but there was no significant effect of the exercise bout. Electrophoretic separation of myosin heavy chain (MHC) isoforms showed the older subjects to have a lower (P < 0.05) percentage of MHC-II isoforms than the young subjects. However, no association was observed between the composition of the muscle and changes in the IGF-I isoforms with exercise. The data from this study show an attenuated MGF response to high resistance exercise in the older subjects, indicative of age-related desensitivity to mechanical loading. The data in young subjects indicate that the MGF and IGF-IEa isoforms are differentially regulated in human skeletal muscle.

    Nat Genet. 2001 Feb;27(2):195-200. Related Articles, Links

    Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle.

    Musaro A, McCullagh K, Paul A, Houghton L, Dobrowolny G, Molinaro M, Barton ER, Sweeney HL, Rosenthal N.

    Cardiovascular Research Center, Massachusetts General Hospital-East, Charlestown, Massachusetts, USA.

    Aging skeletal muscles suffer a steady decline in mass and functional performance, and compromised muscle integrity as fibrotic invasions replace contractile tissue, accompanied by a characteristic loss in the fastest, most powerful muscle fibers. The same programmed deficits in muscle structure and function are found in numerous neurodegenerative syndromes and disease-related cachexia. We have generated a model of persistent, functional myocyte hypertrophy using a tissue-restricted transgene encoding a locally acting isoform of insulin-like growth factor-1 that is expressed in skeletal muscle (mIgf-1). Transgenic embryos developed normally, and postnatal increases in muscle mass and strength were not accompanied by the additional pathological changes seen in other Igf-1 transgenic models. Expression of GATA-2, a transcription factor normally undetected in skeletal muscle, marked hypertrophic myocytes that escaped age-related muscle atrophy and retained the proliferative response to muscle injury characteristic of younger animals. The preservation of muscle architecture and age-independent regenerative capacity through localized mIgf-1 transgene expression suggests clinical strategies for the treatment of age or disease-related muscle frailty.
    *** This paper has a good diagram of the different exons used for the splice variants

    J Cell Biol. 2002 Feb 18;156(4):751-60. Epub 2002 Feb 11. Related Articles, Links

    Different modes of hypertrophy in skeletal muscle fibers.

    Paul AC, Rosenthal N.

    Mouse Biology Program, European Molecular Biology Laboratory, 00016 Monterotondo-Scalo, Rome, Italy.

    Skeletal muscles display a remarkable diversity in their arrangement of fibers into fascicles and in their patterns of innervation, depending on functional requirements and species differences. Most human muscle fascicles, despite their great length, consist of fibers that extend continuously from one tendon to the other with a single nerve endplate band. Other mammalian muscles have multiple endplate bands and fibers that do not insert into both tendons but terminate intrafascicularly. We investigated whether these alternate structural features may dictate different modes of cell hypertrophy in two mouse gracilis muscles, in response to expression of a muscle-specific insulin-like growth factor (IGF)-1 transgene (mIGF-1) or to chronic exercise. Both hypertrophic stimuli independently activated GATA-2 expression and increased muscle cross-sectional area in both muscle types, with additive effects in exercising myosin light chain/mIGF transgenic mice, but without increasing fiber number. In singly innervated gracilis posterior muscle, hypertrophy was characterized by a greater average diameter of individual fibers, and centralized nuclei. In contrast, hypertrophic gracilis anterior muscle, which is multiply innervated, contained longer muscle fibers, with no increase in average diameter, or in centralized nuclei. Different modes of muscle hypertrophy in domestic and laboratory animals have important implications for building appropriate models of human neuromuscular disease

    Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15603-7. Related Articles, Links

    Viral mediated expression of insulin-like growth factor I blocks the aging-related loss of skeletal muscle function.

    Barton-Davis ER, Shoturma DI, Musaro A, Rosenthal N, Sweeney HL.

    Department of Physiology, A700 Richards Building, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085, USA.

    During the aging process, mammals lose up to a third of their skeletal muscle mass and strength. Although the mechanisms underlying this loss are not entirely understood, we attempted to moderate the loss by increasing the regenerative capacity of muscle. This involved the injection of a recombinant adeno-associated virus directing overexpression of insulin-like growth factor I (IGF-I) in differentiated muscle fibers. We demonstrate that the IGF-I expression promotes an average increase of 15% in muscle mass and a 14% increase in strength in young adult mice, and remarkably, prevents aging-related muscle changes in old adult mice, resulting in a 27% increase in strength as compared with uninjected old muscles. Muscle mass and fiber type distributions were maintained at levels similar to those in young adults. We propose that these effects are primarily due to stimulation of muscle regeneration via the activation of satellite cells by IGF-I. This supports the hypothesis that the primary cause of aging-related impairment of muscle function is a cumulative failure to repair damage sustained during muscle utilization. Our results suggest that gene transfer of IGF-I into muscle could form the basis of a human gene therapy for preventing the loss of muscle function associated with aging and may be of benefit in diseases where the rate of damage to skeletal muscle is accelerated.

    Acta Physiol Scand. 1999 Dec;167(4):301-5. Related Articles, Links

    Contribution of satellite cells to IGF-I induced hypertrophy of skeletal muscle.

    Barton-Davis ER, Shoturma DI, Sweeney HL.

    Department of Physiology, A700 Richards Bldg., University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085, USA.

    Insulin-like growth factor I (IGF-I) is critical in promoting growth of skeletal muscle. When IGF-I is introduced into mouse hindlimb muscles by viral-mediated gene transfer, local overexpression of IGF-I produces significant increases in muscle mass and strength compared with untreated controls (Barton-Davis et al. 1998). We have proposed that this functional hypertrophy is primarily owing to the activation of satellite cells which leads to increased muscle regeneration. In order to test if satellite cells are essential in mediating the hypertrophic effects of IGF-I, we used gamma radiation to destroy the proliferative capacity of satellite cells. The right hindlimbs of adult C57BL/6 male mice were subjected to one of the following treatments: (1) 2,500 rad gamma radiation only, (2) viral-mediated gene transfer of IGF-I only, (3) 2,500 rad gamma radiation plus viral-mediated gene transfer of IGF-I, or (4) no intervention as a control. Approximately 4 months after treatment, the extensor digitorum longus muscles (EDL) from both hindlimbs were removed for mechanical and morphological measurements. Treatment with gamma radiation significantly prevented normal growth of the muscle. When combined with IGF-I treatment, approximately half of the IGF-I effect was prevented by gamma radiation treatment. This suggests that the remaining half of IGF-I induced hypertrophy is owing to paracrine/autocrine effects on the adult myofibres. Thus, these data are consistent with a mechanism by which IGF-I induced muscle hypertrophy via a combination of satellite cell activation and increasing protein synthesis in differentiated myofibres

  13. Quote Originally Posted by einstein1905

    I'd gladly post some references w/abstracts if you'd like. Lots of good stuff. The most recent, 3-2004 paper is most relevant to us, as it incorporates resistance training into the equation.

    Awesome. As Manbeast said post everything you have. The more info we have the better. I always enjoy reading anything relevant to this topic.

    I know some people that have done it both ways and like usual you have some that say there is a difference and others that say there isn't. Maybe I'll try IM shots next cycle to see if I notice anything.
    For answers to board issues, read the Suggestion and News forum at the bottom of the main page.

  14. Quote Originally Posted by Bobo
    Awesome. As Manbeast said post everything you have. The more info we have the better. I always enjoy reading anything relevant to this topic.

    I know some people that have done it both ways and like usual you have some that say there is a difference and others that say there isn't. Maybe I'll try IM shots next cycle to see if I notice anything.
    My rationale for going IM bilaterally post workout is....It's been shown that IGF receptors are upregulated in response to resistance training post workout in the muscles worked.....by shooting bilaterally to the muscles worked post workout, you're at least, kinetically, allowing for a higher percentage of desirable bindings. By shooting subQ, you allow IGF-1 to go systemic and bind in a more random fashion. The intestinal epithelia has the highest concentration of IGF receptors, so you're allowing for a greater probability that the IGF-1 will preferentially bind there first. I had great results going IM bilaterally 1x/day with 25mcg/side. Most of the people I know using it are going IM now. I'm new over hear, but are most of you guys reconstituting in BA or 10mM HCl or something else?

  15. BA seems to be the going solvent..

  16. Here's something on the small intestine and LR3 IGF-1

    The role of insulin-like growth factors in small intestinal cell growth and development.

    MacDonald RS.

    Nutritional Sciences Program, University of Missouri, Columbia, USA. [email protected]

    IGF-I and IGF-II receptors are expressed in the small intestine of mammalian species, as are the genes to synthesize both peptides. IGF binding proteins are also expressed in the intestine. IGF-I and IGF-II mRNA are highest in fetal and newborn tissues and decrease with age. IGF-I mRNA is present in the adult small intestine, and is associated with the submucosal regions and crypt cells. IGF-I and IGF-II receptor binding to the small intestine is higher in newborn animals and decreases with age. Both receptors are more concentrated in the crypt than villus regions, but IGF-II binding is higher than IGF-I in all regions. IGF-I receptors are associated with the submucosal region of the small intestine, whereas IGF-II receptors are more abundant in the mucosal cells. Administration of IGF-I either orally or by osmotic pump generally has no affect on small intestinal weight or length, but does increase mucosal cellularity. LR3-IGF-I administration by osmotic pump affects the small intestine similarly to IGF-I, although with a higher potency. In the few studies in which IGF-II was administered, increased gut mass was observed in adult rats, but not newborn rats or pigs. Significant effects on mucosal expression of disaccharidases was achieved with either oral or subcutaneous IGF-I or oral IGF-II. Administration of IGF in models of intestinal hypertrophy and atrophy are also reviewed.


  17. Here's 1 on hIGf-1 being reconstituted in BA got this from einstien

    Pharmaceutical Research. Vol. 14, No.5. 1997

    Solvent Effects on the Solubility and Physical Stability of Human Insulin- Like Growth Factor I

    Purpose. The solubility and physical stability of human Insulin-like Growth Factor I (hIGF-l) were studied in aqueous solutions with differ- ent cxcipients.

    Methods. The solubility of hlGP-r was determined by UV-absorption and quantification of light blocking particles. The physical stability of hlGF-r was studied with differential scanning caJorimetry (DSC) and circular dichroism (CD) spectroscopy.

    Results. Human IGF-l precipitated at Jow temperature in the presence of J40 mM benzyl alcohol and 145 mM sodium chloride. CD data showed that the tertiary structure of hIGF-I during these condions was perturbed compared to that in 5 mM phosphate buffer. In the presence of benzyl alcohol 290 mM mannitol stabilized hIGF-I. Sodium chloride or mannitol by themselves had no effect on either the solubility or the tertiary structure. Benzyl alcohol was attracted to hIGF-l, whereas sodium chloride was preferentially excluded The attraction of benzyl alcohol WIlS reinforced by sodium chloride leading to salting-out of hlGF-l. The CD-data indicated interactions of benzyl alcohol with phenylalanine in hIGF-i. Thermal denaturation of hIGF-I occurred in all solutions with sodium chloride. whereas mannitol or benzyl alcohol had no effect on the thermal stability. The thermal stability of hIGF- I WIlS thus decreased in 145 mM sodium chloride although it WIlS excluded from hIGF-I.

    Conclusions. The self-association and thermal aggregation of hIGF-I is driven by hydrophobic interactions. Benzyl alcohol is attracted to hIGF-I and induces changes in the tertiary structure causing hydropho- bic attraction of the protein at low temperatures.

    Jonas Fransson,1,2,4 Dan Hallen,3 and Ebba Florin-Robertsson, 1

    Received October 29, 1996; accepted February 19. 1997

    1 Department of Pharmaceutical Technology, Pharmacia & upjohn, S-112 87 Stockholm, Sweden

    2 Department of Pharmaceuticlas, Faculty of Pharmacy, Uppsala University, Box 570, S-751 23 Uppsala, Sweden

    3 Department of Structural Chemistry, Parmacia & Upjohn, S-112 87 Stockholm, Sweden

    4 To whom correspondence should be addressed. (e-mail: [email protected])


  18. Long™R3IGF-I
    Recombinant analog of human insulin growth factor-I


    Long™R3IGF-I is a recombinant analog of human insulin-like growth factor-I (IGF-I) that has been specifically engineered for the enhancement of cell culture performance. Long™R3IGF-I is more biologically potent in vitro than either insulin or native IGF-I and has been documented to
    significantly increase recombinant protein production. It is ideal for both research and large-scale culture systems utilizing serum-free or low-level serum applications. Long™R3IGF-I is effective in any cell that contains type I IGF receptors, including most Chinese Hamster Ovary (CHO) lines, hybridomas and fibroblasts. Long™R3IGF-I is produced in a patented E. coli expression system without the use of animal-derived components.


    This product is for research/laboratory use. THIS PRODUCT


    Long™R3IGF-I in lyophilized form should be stored at 2 to 8 C and is stable for at least 3 years. Liquid solutions of Long™R3IGF-I (prepared as described below) can be stored
    at 2 to 8 C and are stable for at least 2 years.

    Preparation Instructions

    1. Long™R3IGF-I is supplied lyophilized in an atmosphere of nitrogen at a slight vacuum (-25 kPa). Remove the metal cap from the glass vial and introduce an air filled syringe
    through the septum to equalize the pressure.

    2. Add sufficient 10 mM HCl or 100 mM acetic acid solution to the vial to achieve a peptide concentration of at least 0.1 mg/mL. Concentrations of 1 mg/mL or more are recommended.

    3. Mix the solution thoroughly to insure the peptide is completely dissolved.

    4. Filtration of a Long™R3IGF-I solution or a culture medium after the addition of Long™R3IGF-I should be performed using a low protein-binding membrane such as Polyvinyl Idene Flouride (PVDF), Poly Ethylene Sulfite (PES) or Cellulose Acetate (CA).

    Methods for Use

    Once Long™R3IGF-I has been reconstituted, it can then be added directly to cell culture medium. A titration of Long™R3IGF-I should be performed for each different application as the optimum concentration may vary depending upon the cell type used and other components present in the medium. The recommended final concentration range of Long™R3IGF-I is 10 to 50 µg/L (or ng/mL). Because Long™R3IGF-I and insulin may compete for the same cell receptors, the effectiveness of Long™R3IGF-I will be masked if it is added in conjunction with commonly employed concentrations of insulin (1 to 10 mg/L). However, inclusion of physiological levels of insulin (5 to 10 µg/L) in cell culture medium containing the recommended levels of
    Long™R3IGF-I results in beneficial synergistic effects in certain applications.


    White powder

    Molecular weight
    9110 ± 2 daltons (Mass spectroscopy)

    < 0.1 EU/µg

    Biological Activity
    ED50 < 10 ng/mL (Bioassay assessing the stimulation of
    protein synthesis in L6 myoblasts)

    Confirmed by N-terminal sequence analysis and HPLC

    1. Francis, G., et al. J. Mol. Endocrinol. (1992) 8:213.
    2. Thomas, J., Fung, V. Animal Cell Technology: Products of
    Today, Prospects for Tomorrow (1993) 91.
    3. Morris, A., Schmid, J. Biotechnol. Prog. (2000) 16:693.


  19. Thanks Johnny... Glad to see you over here

  20. Thanks Bro glad to be here, here's a LR3 IGF-1 profile

    Long™R3 IGF-I
    Good Science. Great Performance.

    The efficient and effective manufacture of recombinant proteins, antibodies, vaccines and viral products in animal cells requires a source of growth factors or some means of growth factor signaling to cells. The traditional method is to provide an external source of growth factors, primarily through the addition of fetal bovine serum to culture media. However, many sectors of the biotechnology
    and pharmaceutical industries are now demanding pure recombinant growth factors, made under the highest quality standards, or inclusion in serum-free media formulations.

    The insulin-like growth factors (IGFs) were originally discovered and purified from serum. They are considered to be important growth factors for industrial cell culture because:

    • They are present in all animal and human sera at concentrations of 100 - 500 µg/L.

    • The removal of IGFs from serum can abolish up to 90% of the cell growth-promoting activity.

    • They stimulate nutrient uptake, cell growth, protein synthesis and inhibit apoptosis or programmed cell death in a wide range
    of cell types.

    • Almost all cells have type I IGF receptors, which mediate the biological action of IGFs.

    Many industrially important cell types can be cultured in serum-free media that contain high concentrations of insulin (5 - 10 mg/L). This is about 1000-fold higher than the normal physiological concentration of insulin. Insulin only works in cell culture because it acts as a weak substitute for IGFs. Much lower levels of IGFs can replace insulin.

    The insulin-like growth factors are structurally related to insulin. There are two forms, IGF-I and IGF-II, which are similar and have closely related actions on cell growth via the same receptor. IGF-I is considered to be the main post-natal growth-promoting factor and IGF-II has major effects during fetal development. IGF-I is a non-glycosylated, single chain polypeptide 70 amino acids in length.

    Structure of IGF-I and Insulin
    Insulin-like growth Factor-I Insulin

    IGF-I is similar in structure to pro-insulin, the precursor of insulin. Pro-insulin is a single chain polypeptide, which is cleaved to remove the connecting C peptide, to form insulin. Insulin has two chains (A and B chain) connected by two disulphide bonds.

    The receptors for IGF-I and insulin are also structurally related and both ligands interact with each other’s receptors with very low affinity. In cell culture, the potency of IGF-I is higher than insulin because the cellular responses required for biopharmaceutical production in animal cells are mediated via the type I IGF receptor, not the insulin receptor.

    Another important feature is that a family of six IGF binding proteins regulates the biology of IGF peptides. These proteins are found in serum and are also produced by cells in culture. IGF binding proteins bind IGFs with high affinity and generally inhibit the actions of IGFs on cells. This has been exploited by making analogs of IGF peptides that do not bind to IGF binding proteins and are therefore superior to both IGF-I and insulin in cell culture. The most potent of these analogs for commercial cell culture purposes is LongR3 IGF-I.

    LongR3 IGF-I
    LongR3 IGF-I has been specifically engineered and manufactured by GroPep Limited for use in serum-free cell culture media. Structurally it has two significant modifications — first, one amino acid in the IGF-I structure, the glutamic acid (E) at position 3 has been replaced with an arginine (R), which accounts for the R3 in the name; and second, because the molecule is made as a fusion protein, it has an N-terminal fusion partner which is 13 amino acids long. Thus the “Long” in the name.

    Structure of LongR3 IGF-I

    Replacing the glutamic acid (E) with arginine (R) at position 3 is important because this modification significantly reduces the binding of the growth factor to the IGF-I binding proteins, enabling LongTMR3IGF-I to be so potent. The addition of the fusion partner also enhances refolding and facilitates high-yield production. The end result is a growth factor 10-fold more potent in cultured cells compared to native IGF-I and 200- to 1000-fold more potent than insulin.

    LongR3 IGF-I is manufactured in genetically engineered E. coli. The manufacturing process uses no animal sourced material, making it regulatory friendly for commercial biopharmaceutical production. The system of production is briefly outlined below:

    1. Fermentation. E. coli containing the gene for LongR3 IGF-I are grown in a fermenter. GroPep Limited’s patented expression system uses inclusion body technology.

    2. Homogenization. Bacteria are lysed to release inclusion bodies that are harvested by differential centrifugation.

    3. Dissolution. The recombinant fusion protein is released into solution. It is not correctly folded into its tertiary protein structure at this point.

    4. Refolding. The LongR3 IGF-I protein is incubated under controlled conditions so that the
    disulphide bonds can correctly form to allow the correct protein structure. The protein would be biologically inactive or less active in an incorrectly folded form.

    5. Purification. A four-step system is used to purify LongR3 IGF-I. This series of steps also incorporates accepted protocols for the removal of bacterial endotoxin.

    6. Supply. The product is subjected to quality control assays and is available as a lyophilized powder or can be manufactured as a liquid for delivery to customers.

    It is important to be aware that insulin is acting in cell culture systems as a weak analog of IGF-I. LongR3 IGF-I will therefore work in any serum-free medium or cell culture system in which insulin is used. The potency compared to insulin is best illustrated by the data published by Morris, et al, 20001. They found that LongR3 IGF-I was superior to insulin in terms of recombinant protein production, primarily by increasing the number of viable Chinese Hamster Ovary (CHO) cells in a small production system. LongR3 IGF-I was used in the µg/L range compared to insulin in the mg/L concentration range.

    Advantages of LongR3 IGF-I

    There are several advantages to using LongR3 IGF-I in cell culture rather than insulin.

    1. LongR3 IGF-I is Better Cell Science. Because LongR3 IGF-I acts directly on the type I IGF receptor it is the right tool for the job. And since far less LongR3 IGF-I is required in media than insulin it can make downstream processing easier and more efficient as well.

    2. LongR3 IGF-I Outperforms Insulin. Published research has shown that LongR3 IGF-I leads to overall greater productivity by increasing cell viability and delaying programmed cell death.

    3. LongR3 IGF-I is Readily Available and Regulatory Friendly. Since LongR3 IGF-I is a recombinant protein manufactured in a process without any animal-derived components it eliminates regulatory concerns. It is a proven cell culture product currently employed in the manufacturing process of a number of FDA-approved biopharmaceuticals. A secure and ample manufacturing capacity ensures a continual, ready supply for commercial production needs.

    4. LongR 3IGF-I is Less Expensive than Insulin. Depending on the amount of LongR3 IGF-I used to achieve cell growth, and the productivity enhancements one achieves, LongTMR3IGF-I can be significantly less expensive than insulin on a dollar/liter basis as shown on the chart below. Also, over time, as LongR3 IGF-I usage increases, the cost of production will decrease – making it even less expensive, while insulin costs have been steadily increasing.

    Preparation and use of LongR3 IGF-I

    LongR3 IGF-I is supplied as a freeze-dried formulation or as a liquid.

    The freeze-dried formulation is packed in an atmosphere of nitrogen at a slight vacuum. To prepare a solution for cell culture, introduce an air filled syringe through the septum to equalize the pressure. Next, add sufficient 10 mM HCl or 100 mM acetic acid to the vial to achieve a peptide concentration of at least 0.1 mg/mL. Concentrations of 1 mg/mL or more are recommended. Mix the solution thoroughly to ensure the peptide is completely dissolved. The solution can then be filtered through a low-protein binding membrane before addition to cell culture medium or it can be added directly to the medium, which can subsequently be filtered.

    The liquid product is formulated in acetic acid (100 mM) at a concentration of 5 - 7 g/L and is ready to dilute straight into cell culture medium to achieve a biologically active concentration of about 50 µg/L. The final dilution of 100,000-fold, means that there is no effect on pH or osmolality of the cell culture medium.

    A titration for LongR3 IGF-I should be performed for each different application as the optimum concentration may vary slightly depending upon the cell type used and other components present in the medium. The recommended final concentration range of LongR3 IGF-I is 10 to 50 µg/L.

    Because LongR3 IGF-I and insulin act through the same cell receptor, the effectiveness of LongR3 IGF-I will be masked if it is added in conjunction with commonly employed concentrations of insulin (~10 mg/L). However, inclusion of physiological levels of insulin (~5 µg/L) in cell culture medium containing the recommended levels of LongR3 IGF-I can result in beneficial synergistic effects in certain applications.


  21. Great info Johnny. Welcome.
    For answers to board issues, read the Suggestion and News forum at the bottom of the main page.

  22. I'm still looking for information on why it can only be used for 30 days. I know the theory but I can't find any study that confirms this. Hey Johnny I know you've had experience with IGF-1, do you know of anyone that has used this longer than 4 weeks with results?
    For answers to board issues, read the Suggestion and News forum at the bottom of the main page.

  23. Quote Originally Posted by Bobo
    I'm still looking for information on why it can only be used for 30 days. I know the theory but I can't find any study that confirms this. Hey Johnny I know you've had experience with IGF-1, do you know of anyone that has used this longer than 4 weeks with results?
    I know of a few people that have, and everyone seems to say the same thing: the effects drastically taper as you go beyond 4-5 weeks. I still swear by receptor downregulation rather than any of the other theories. Also, doses above 80mcg or so don't seem to be any better than doses below 80mcg/day. So, more is better doesn't really apply here either. Since IGF-1 upregulates insulin receptors and insulin upregulates IGF-1 receptors (both initially, and probably the opposite occurs over time), and each has some affinity for the other's receptors, to some degree, it probably wouldn't be beneficial to alternate IGF-1-insulin cycles, as that would seem to lower sensitivity to each. While using them in conjunction may lead to quicker desensitization, it may still be worth it due to the great potential synergistic efects.

  24. Thanks for the explanation. I wish I could get something concrete on this OR find some way that use can continue over the 4 weeks peroid.
    For answers to board issues, read the Suggestion and News forum at the bottom of the main page.

  25. I ran it for 5 weeks at 40mcg, I was still getting results but ran out. I know LA is going to use it for 12 weeks to see what happens.



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