EvoMuse Presents: Epitome™
- Thread starter dsade
- Start date
ThaPeoplesChamp
Member
Went to break at 840am, took my first dose. Break ended at 9am, thought I forgot to take it so took another. It's now 10:15am and I feel like ****. Burning up pouring sweat and shaky. Absolutely no placebo effect, this stuff gets right down to business.
GreenMachineX
Well-known member
Ha, me too.
chedapalooza
Legend
and our first accidental OD report is in
blurryimage
Member
So Thursday was day 8 and my appetite was normal, but like 20 minutes after my last meal of the day I felt super full. I felt like I went to a buffet and way over ate but had only eating the same size meal as the day before. Today my appetite is still crushed. Granted it is only 10:36 am but it was hard to get a small shake down this am. I'll keep an eye on this and see if it continues.
I also tightened my belt a notch and ordered 3 more bottles as I think it is going to seek out fast.
I also tightened my belt a notch and ordered 3 more bottles as I think it is going to seek out fast.
GNO
Well-known member
and our first accidental OD report is in
Was it really accidental? lol
ThaPeoplesChamp
Member
GNO
Well-known member
X2 here. I'm getting warm in the pants readings these observations after 1-2 weeks while I wait for my bottle lol.
GNO
Well-known member
Matt had posted earlier no, but after a while you may get to a point where there is diminishing returns so taking a break would be user specific.
GreenMachineX
Well-known member
Just got home to find a package waiting on me. First capsule of Epitome consumed. 
GreenMachineX
Well-known member
Is there any chance this product could interact with stims, at the least potentiate them? Or give some energy itself? Typically on Friday afternoon I'm beat from the work week but feeling really good right now.
vujade
Well-known member
GreenMachineX
Well-known member
probably because your metabolism is working better
I didn't think it would work so quickly though... If that's really what's happening, I'm game. I am definitely one of those endomorphs described in the writeup (tired and lethargic from dieting, wanting to just lay around and eat).
dsade
NutraPlanet Fanatic
I knew it was going to be decently quick both based on my experience with the original Leptigen Rebirth, and the details of the studies we cited - but I would never have thought it would be THIS powerful.
We didn't even need to alpha or beta test this formula to know it would be impressive.
I went ahead and ordered everything I need to do a second run....first run is SOLD OUT except for some retailers and a few bottles left at my store.
GNO
Well-known member
Personally I would have lied and said it was exactly what I planned it to be lol
GNO
Well-known member
Well it is, but it has been over a decade since we had Rebirth to play with, and I have become more of an endomorph than before, which makes the results that more stunning.
Nice! Still waiting on my bottle to log, but am sitting at closer to 13% and trying to work it down by the time it shows up.
Want me to wait until 12% or start when it arrives?
GNO
Well-known member
I got a notice when I got home that it's waiting at the post office. I'll pick it ip tomorrow and get the log up by Sunday.
taman6886
Well-known member
No need to cycle.
ThaPeoplesChamp
Member
I said I wouldn't talk about results till I was done. I lied. Definitely leaning out. Not dramatic yet but enough that a casual glance last night in the mirror gave me a holy poop moment. I'm a week in.
Get that second run going, I'll be passing my overtime checks to you for it.
Get that second run going, I'll be passing my overtime checks to you for it.
abformulations
Legend
Lol. This product seems like a winner so far. Can't wait till a month is in the books for everyone.
GNO
Well-known member
I like 7's ... it's skinny jean season lol.
blurryimage
Member
Big stars are good for big thighs, but they cost, but they look good lol
dsade
NutraPlanet Fanatic
I might look up some more of the Buffalo with the elastic in them. The 33s are too loose in the waist as of today.
GNO
Well-known member
Haha I'm also short and on the lean side but after I ran BMP and then myosynergy+ARA my quads exploded. All my 7's are tight but still fit
dsade
NutraPlanet Fanatic
Pervert
GNO
Well-known member
Lol, at least thrown a 1 in front of the 7
GNO
Well-known member
Why stop at three? If epitome expedites my cut it will be all out mayhem.
taman6886
Well-known member
I have type II diabetes and my blood sugar readings have been bad the last few months. On day 2, my morning reading dropped from 273 to 215. Not ideal by any stretch, but a great improvement. I also noted fewer food cravings and that I am satiated more quickly and for longer when feeding.
GreenMachineX
Well-known member
I've taken 3 doses so far, and I haven't noticed any effects on appetite or satiation (or satiety?) yet. But, I do feel I'll need to lower my dose of stims as there's a pretty strong surge of "energy" when I take that cap in the morning. Anyone else notice that?
ryanp81
Well-known member
Not only that but anyone notice pain reducing effects ? I've had a nagging shoulder and bicep pain and it seems to be diminished, knees feel good as well.
ThaPeoplesChamp
Member
The extra body heat has been getting worse, not intolerable but at times uncomfortable.
The last time I felt like this was on DNP. And to a lesser extent sodium usniate/usnic acid.
It's a good thing.
The last time I felt like this was on DNP. And to a lesser extent sodium usniate/usnic acid.
It's a good thing.
blurryimage
Member
Matt, I need some help understanding epitome a little more. I am still not clear on how I am loosing body fat and my jeans fit looser, but I am not loosing body weight. I don't feel like I'm eating enough right now to be gaining muscle while loosing fat but maybe I am. Or is this some kind of tissue alchemy where it turns fat to muscle.
I don't mind that I stay at 220lbs and just lean up but I just didn't really think it was possible.
I don't mind that I stay at 220lbs and just lean up but I just didn't really think it was possible.
PharmAnalyst
Member
I'm noticing much of the same. Even with mild TTA bloat my clothes are undoubtedly fitting much more loosely.
Eclectic9kid
New member
Exact same thing here.. Kinda weird.
dsade
NutraPlanet Fanatic
I'm going to post this teaser up...there is an explanation in here, but I will be doing two things:
1) Applying some new hypothesis to an enhanced CardioTryx formula
2) having Marc do a dietary accompaniment/timing guide for maximum fat loss/muscle gain while incorporating Epitome and Rebirth (along with the other two Leptigen formulas)
Proceedings of The Physiological Society
Cardiovascular nutrigenomics: from kitchen to bedside Abstracts
University of Oxford (2008) Proc Physiol Soc 12, SA10
Research Symposium
AMPK: a sensor of glycogen as well as AMP and ATP?
D. G. Hardie1
1. Division of Molecular Physiology, University of Dundee, Dundee, United Kingdom.
Medline articles by:
Hardie, DG
The classical view of the AMP-activated protein kinase (AMPK) system is that it is a sensor of energy that monitors the cellular concentrations of AMP and ATP, and which regulates energy balance by stimulating catabolism and inhibiting anabolism whenever the cellular AMP:ATP ratio rises [1]. The kinase is a heterotrimeric complex of a catalytic α subunit and regulatory β and γ subunits. The γ subunits contain two tandem domains that bind the regulatory nucleotides, AMP and ATP, in a mutually exclusive manner. The kinase is only active after phosphorylation at a conserved threonine residue in the α subunit (Thr-172) by upstream kinases, of which the most important is the tumour suppressor LKB1. LKB1 appears to phosphorylate Thr-172 continually, but binding of AMP (but not ATP) to the γ subunit inhibits Thr-172 dephosphorylation. Since any fall in the cellular ATP:ADP ratio is amplified by adenylate kinase into a much larger rise in the AMP:ATP ratio, this mechanism acts as a sensitive switch that converts the kinase into its active, phosphorylated form. In addition, the phosphorylated kinase is allosterically activated 10-fold by AMP binding; the combined effects of phosphorylation and allosteric activation result in >1000-fold activation. In some cells, Thr-172 can also be phosphorylated by CaMKKβ, a calmodulin-dependent protein kinase. This occurs in response to a rise in intracellular Ca2+ and does not require any increase in AMP. The β subunits of the AMPK heterotrimer contain a central glycogen-binding domain (GBD) that is conserved in all eukaryotic orthologues. Although this domain is known to cause binding of AMPK to glycogen in intact cells [2,3], its physiological function has been unclear. We have now shown that it is a regulatory domain and that binding of glycogen to it causes allosteric inhibition of AMPK. Glycogen is a polymer of glucose units joined by α1-4 linkages, with occasional branches formed by α1-6 linkages. A major problem with the study of glycogen as a regulatory molecule is that it does not have a defined structure, but varies both in size and branching content. Based on findings suggesting that the degree of branching affected its inhibitory potency, we have synthesized small α1-4 linked glucose oligosaccharides containing single α1-6 branches, and have shown that these are potent allosteric inhibitors of AMPK. The most potent oligosaccharide gives half-maximal inhibition at 90 μM, and also markedly inhibits phosphorylation of Thr-172 by LKB1 and CaMKKβ. Inhibition is due to binding to the GBD, because point mutations in the latter than abolish glycogen binding also abolish inhibition. One of the physiological targets of AMPK is muscle glycogen synthase (mGS), which is inactivated by phosphorylation at Ser-7 [4]. A curious paradox is that although AMPK is activated by ATP depletion during exercise, mGS is usually found to be dephosphorylated and activated following exercise, as long as the exercise had been sufficiently prolonged to cause significant glycogen depletion. We believe that the regulation of AMPK via the GBD may explain this paradox. The outer tier of glycogen (representing the glucose that can be released by glycogen phosphorylase without the need for the action of debranching enzyme) contains up to one third of all of the glucose units in a single molecule. Theoretical studies suggest that in a fully synthesized molecule of glycogen the outer chains are so tightly packed that the branch points would not be accessible. We suspect that under these conditions AMPK binds to glycogen but is not inhibited, so that it would phosphorylate mGS, thus exerting a feedback inhibition of further extension of the outer chains of glycogen. We also propose that when exercise commences, phosphorylase removes some of the outer chains, exposing the branch points which would then bind AMPK and cause inhibition. mGS would now be dephosphorylated and activated by the glycogen-bound forms of protein phosphatase-1, so that it was ready to replenish glycogen stores as soon as exercise ceased. This hypothesis may also explain why insulin-stimulated glucose uptake and glycogen synthesis is enhanced following a single bout of exercise, as long as the exercise bout was sufficient to cause significant glycogen depletion. It can also answer another unsolved question: how do cells "know" when their glycogen stores are sufficient, and conversely how do they "know" when they are insufficient and need replenishing? These are important questions because insulin resistance, the primary cause of type 2 diabetes and the metabolic syndrome, can be viewed as a mechanism to limit the amount of nutrient that cells can store
1) Applying some new hypothesis to an enhanced CardioTryx formula
2) having Marc do a dietary accompaniment/timing guide for maximum fat loss/muscle gain while incorporating Epitome and Rebirth (along with the other two Leptigen formulas)
Proceedings of The Physiological Society
Cardiovascular nutrigenomics: from kitchen to bedside Abstracts
University of Oxford (2008) Proc Physiol Soc 12, SA10
Research Symposium
AMPK: a sensor of glycogen as well as AMP and ATP?
D. G. Hardie1
1. Division of Molecular Physiology, University of Dundee, Dundee, United Kingdom.
Medline articles by:
Hardie, DG
The classical view of the AMP-activated protein kinase (AMPK) system is that it is a sensor of energy that monitors the cellular concentrations of AMP and ATP, and which regulates energy balance by stimulating catabolism and inhibiting anabolism whenever the cellular AMP:ATP ratio rises [1]. The kinase is a heterotrimeric complex of a catalytic α subunit and regulatory β and γ subunits. The γ subunits contain two tandem domains that bind the regulatory nucleotides, AMP and ATP, in a mutually exclusive manner. The kinase is only active after phosphorylation at a conserved threonine residue in the α subunit (Thr-172) by upstream kinases, of which the most important is the tumour suppressor LKB1. LKB1 appears to phosphorylate Thr-172 continually, but binding of AMP (but not ATP) to the γ subunit inhibits Thr-172 dephosphorylation. Since any fall in the cellular ATP:ADP ratio is amplified by adenylate kinase into a much larger rise in the AMP:ATP ratio, this mechanism acts as a sensitive switch that converts the kinase into its active, phosphorylated form. In addition, the phosphorylated kinase is allosterically activated 10-fold by AMP binding; the combined effects of phosphorylation and allosteric activation result in >1000-fold activation. In some cells, Thr-172 can also be phosphorylated by CaMKKβ, a calmodulin-dependent protein kinase. This occurs in response to a rise in intracellular Ca2+ and does not require any increase in AMP. The β subunits of the AMPK heterotrimer contain a central glycogen-binding domain (GBD) that is conserved in all eukaryotic orthologues. Although this domain is known to cause binding of AMPK to glycogen in intact cells [2,3], its physiological function has been unclear. We have now shown that it is a regulatory domain and that binding of glycogen to it causes allosteric inhibition of AMPK. Glycogen is a polymer of glucose units joined by α1-4 linkages, with occasional branches formed by α1-6 linkages. A major problem with the study of glycogen as a regulatory molecule is that it does not have a defined structure, but varies both in size and branching content. Based on findings suggesting that the degree of branching affected its inhibitory potency, we have synthesized small α1-4 linked glucose oligosaccharides containing single α1-6 branches, and have shown that these are potent allosteric inhibitors of AMPK. The most potent oligosaccharide gives half-maximal inhibition at 90 μM, and also markedly inhibits phosphorylation of Thr-172 by LKB1 and CaMKKβ. Inhibition is due to binding to the GBD, because point mutations in the latter than abolish glycogen binding also abolish inhibition. One of the physiological targets of AMPK is muscle glycogen synthase (mGS), which is inactivated by phosphorylation at Ser-7 [4]. A curious paradox is that although AMPK is activated by ATP depletion during exercise, mGS is usually found to be dephosphorylated and activated following exercise, as long as the exercise had been sufficiently prolonged to cause significant glycogen depletion. We believe that the regulation of AMPK via the GBD may explain this paradox. The outer tier of glycogen (representing the glucose that can be released by glycogen phosphorylase without the need for the action of debranching enzyme) contains up to one third of all of the glucose units in a single molecule. Theoretical studies suggest that in a fully synthesized molecule of glycogen the outer chains are so tightly packed that the branch points would not be accessible. We suspect that under these conditions AMPK binds to glycogen but is not inhibited, so that it would phosphorylate mGS, thus exerting a feedback inhibition of further extension of the outer chains of glycogen. We also propose that when exercise commences, phosphorylase removes some of the outer chains, exposing the branch points which would then bind AMPK and cause inhibition. mGS would now be dephosphorylated and activated by the glycogen-bound forms of protein phosphatase-1, so that it was ready to replenish glycogen stores as soon as exercise ceased. This hypothesis may also explain why insulin-stimulated glucose uptake and glycogen synthesis is enhanced following a single bout of exercise, as long as the exercise bout was sufficient to cause significant glycogen depletion. It can also answer another unsolved question: how do cells "know" when their glycogen stores are sufficient, and conversely how do they "know" when they are insufficient and need replenishing? These are important questions because insulin resistance, the primary cause of type 2 diabetes and the metabolic syndrome, can be viewed as a mechanism to limit the amount of nutrient that cells can store