BCAA Ethyl Ester (BCAAE2™) Highlights:
- Potent anabolic activity to increase muscle growth
- Increased Protein Synthesis and Nitrogen Retention by
turning on anabolic genes
- Increase the important anabolic hormones insulin, GH, and
- Potent anti-catabolic activity to inhibit muscle breakdown
- Muscle sparing
- Glycogen sparing
- Improved and increased muscle recovery
- Lower lactate production
- Dramatically more potent than regular BCAA's and metabolites like a-ketoisocaproic acid
- Unmatched BCAA absorption and utilization (bioavailability)
Branched Chain Amino Acids (BCAA's)
function by increasing protein synthesis and nitrogen retention. Athletes and
bodybuilders recognize that protein synthesis and nitrogen retention are
important anabolic functions required for muscle growth, but many don’t realize
how these compounds work.
BCAAE2™ turns on the genes necessary for protein synthesis and muscle anabolism
in muscle through non-hormonal anabolic action. They work by turning on the main
protein synthesis pathway called mTOR. mTOR is a very important biochemical
pathway that acts as the main signal to tell your muscle cells to increase
protein synthesis. When the mTOR pathway is activated it signals your muscles to
enter an anabolic state and start building muscle. This will allow you to reach
your genetic potential and build new slabs of muscle.
BCAAE2™ also increases the release of hormones such as insulin, growth hormone (GH),
and IGF-1. These hormones are the main anabolic hormones your body uses to
increase muscle protein synthesis, and when these hormones are high there is a
synergistic anabolic effect with sufficient BCAA. Axis Labs® BCAAE2™ will make
sure that your body is in anabolic mode and fuel muscle growth like nothing you
have experienced before. Supplementing with BCAAE2™ is especially important for
people over the age of 40. Research shows that the muscle anabolism that occurs
following a meal high in protein is reduced in aged muscle. Supplementing with
BCAA can boost muscle anabolism and it will allow older athletes to stay
The benefits of supplementing with BCAAE2™ aren’t limited to muscle anabolism,
these compounds are hugely anti-catabolic and prevent you from wasting your hard
earned muscle. When you exercise strenuously your body is forced to uses
glycogen as fuel, when glycogen is used up your body begins to use muscle as
fuel. BCAAE2™ are unique in that they are primarily metabolized in the muscle.
When metabolized, BCAAE2™ provide the necessary amino acids that your body uses
for gluconeogenesis once the glycogen stores have been used up. Taking BCAAE2™
before strenuous exercise will insure that you don’t use your muscles for fuel.
Because of their anti-catabolic effect BCAA's may also help during extreme
dieting by preventing muscle tissue breakdown. Additionally, BCAAE2™ can aid in
recuperation by decreasing lactic acid levels in muscle cells. This is a great
benefit, and can an athlete reach new levels of workout intensity.
The reason that BCAA supplementation has never been extremely popular among athletes is that their benefit is difficult to realize when taken orally. The problem with traditional BCAA's is that there
is limited absorption through the digestive tract, this has plagued other BCAA
products since they were first released. Regular BCAA's are degraded rapidly,
leaving small amounts of the original dose active. Because of the rapid
breakdown of BCAA's, their ability to promote muscle growth is limited. The
limited potential of BCAA's has historically been a problem, until now.
Axis Labs® BCAAE2™ are an amazing advance in scientific supplement technology,
that are much more effective than traditional BCAA supplements. The Ester-Sorb™
technology we use allows the BCAA's to be much more bioavailable. They are not
broken down by the body as quickly as normal amino acids and they can enter the
blood stream from the GI tract more readily.
The reason BCAAE2™ is much more effective than other BCAA products is because of
the ethyl ester added to each BCAA molecule. In fact, BCAAE2™ utilizes the same
Ester-Sorb™ ethyl ester delivery technology that makes our NE2™ many times more
effective than regular L-Arginine. The ethyl ester makes the BCAA’s less polar
and therefore more easily absorbed in the digestive tract. Because of this
design, each amino acid can pass through the intestine largely intact. The ethyl
ester also protects the BCAA molecules from rapid degradation, making them much
more effective in smaller doses than other BCAA products. BCAAE2™ is superior in
design to all other current BCAA products on the market, including products
containing BCAA metabolites like a-ketoisocaproic acid and after one month of
use, you will never train without them again. BCAAE2™ provides a much more
effective and efficient way to experience the benefits of BCAA supplementation.
If you are ready to take training to the next level and record muscle growth,
then you are ready for BCAAE2™.
As a dietary supplement, take 2 to 4 capsules 1 to 3 times daily, preferably prior to and after exercise and/or with meals.
Store in a cool place. Protect from heat, light and moisture.
I've used bcaa's for years; this is the best deal I have found both in terms of cost and effectiveness of the quality of ingredients. Axis labs really have a solid product here and the key for any supplement regime.
Excellent bcaa product. This is now my sixth attempt at trying to find an effective bcaa supplements and I've finally done it. I've been able to add some extra size thanks to Axis Labs bcaa, and the best part is that it's natural.
Very good product for Strength, and Recovery. It is also very convenient due to being in capsule form. Axis is a very reputable company that I have used numerous times.
In my preparation for my show last year AXIS labs Supplements played an integral role in my contest prep. One of the main products I used was the BCAA Ethyl Ester. The muscle sparing properties are immeasurable when dieting especially for me as I was using a ketogenic diet [ultra low carbs diet]. I used BCAA pills 20 minutes before my cardio first thing in the morning to spare my muscle tissue and also because amino acids are the main nutrient I was using for energy. I also would take 2 after with my first meal of the day. The BCAA really helped my recovery from grueling workouts and also increased my strength and due to the revolutionary development of making them BCAA ethyl ester means that I have to take less and be just as potent as other BCAA products on the market. Try them in your supplement regiment and you will not be disappointed.
Acosta, E. P. and C. V. Fletcher (1997). Valacyclovir. Ann Pharmacother 31(2):
Anthony, J. C., T. G. Anthony, S. R. Kimball, et al. 2001. Signaling pathways
involved in translational control of protein synthesis in skeletal muscle by
leucine. J Nutr 131(3): 856S-860S.
Anthony, J. C., T. G. Anthony and D. K. Layman 1999. Leucine supplementation
enhances skeletal muscle recovery in rats following exercise. J Nutr 129(6):
Bassit, R. A., L. A. Sawada, R. F. Bacurau, et al. 2000. The effect of BCAA
supplementation upon the immune response of triathletes. Med Sci Sports Exerc
Beugnet, A., A. R. Tee, P. M. Taylor, et al. 2003. Regulation of targets of mTOR
(mammalian target of rapamycin) signalling by intracellular amino acid
availability. Biochem J 372(Pt 2): 555-66.
Beaumont, K., R. Webster, I. Gardner and K. Dack (2003). Design of ester
prodrugs to enhance oral absorption of poorly permeable compounds: challenges to
the discovery scientist. Curr Drug Metab 4(6): 461-85.
Bigard, A. X., P. Lavier, L. Ullmann, et al. 1996. Branched-chain amino acid
supplementation during repeated prolonged skiing exercises at altitude. Int J
Sport Nutr 6(3): 295-306.
Blomstrand, E. 2001. Amino acids and central fatigue. Amino Acids 20(1): 25-34.
Blomstrand, E. 2006. A role for branched-chain amino acids in reducing central
fatigue. J Nutr 136(2): 544S-547S.
Blomstrand, E., J. Eliasson, H. K. Karlsson, et al. 2006. Branched-chain amino
acids activate key enzymes in protein synthesis after physical exercise. J Nutr
136(1 Suppl): 269S-73S.
Blomstrand, E., P. Hassmen, B. Ekblom, et al. 1991. Administration of
branched-chain amino acids during sustained exercise--effects on performance and
on plasma concentration of some amino acids. Eur J Appl Physiol Occup Physiol
Blomstrand, E., P. Hassmen and E. A. Newsholme 1991. Effect of branched-chain
amino acid supplementation on mental performance. Acta Physiol Scand 143(2):
Blomstrand, E. and B. Saltin 2001. BCAA intake affects protein metabolism in
muscle after but not during exercise in humans. Am J Physiol Endocrinol Metab
Calvey, H., M. Davis and R. Williams 1985. Controlled trial of nutritional
supplementation, with and without branched chain amino acid enrichment, in
treatment of acute alcoholic hepatitis. J Hepatol 1(2): 141-51.
Campbell, W. W., M. C. Crim, V. R. Young, et al. 1995. Effects of resistance
training and dietary protein intake on protein metabolism in older adults. Am J
Physiol 268(6 Pt 1): E1143-53.
Chang, Y., Kang, S., Ko, S., Park, W. (2006). Pretreatment with
N-nitro-L-arginine methyl ester improved oxygenation after inhalation of nitic
oxide in newborn piglets with Escherichia coli pneumonia and sepsis. J Korean
Medical Science 21: 965-72.
Chawla, W., Stackhouse, J., Wadsworth, A. 1975. Efficiency of a-Ketoisocaproic
Acid as a Substitute for Leucine in the Diet of the Growing Rat. J Nutr 105(6):
Cota, D., K. Proulx, K. A. Smith, et al. 2006. Hypothalamic mTOR signaling
regulates food intake. Science 312(5775): 927-30.
De Clercq, E. and H. J. Field (2006). Antiviral prodrugs - the development of
successful prodrug strategies for antiviral chemotherapy. Br J Pharmacol 147(1):
De Palo, E. F., R. Gatti, E. Cappellin, et al. 2001. Plasma lactate, GH and
GH-binding protein levels in exercise following BCAA supplementation in
athletes. Amino Acids 20(1): 1-11.
Eksborg, S., N. Pal, M. Kalin, C. Palm and S. Soderhall (2002). Pharmacokinetics
of acyclovir in immunocompromized children with leukopenia and mucositis after
chemotherapy: can intravenous acyclovir be substituted by oral valacyclovir? Med
Pediatr Oncol 38(4): 240-6.
Garlick, P. J., M. A. McNurlan and C. S. Patlak 1999. Adaptation of protein
metabolism in relation to limits to high dietary protein intake. Eur J Clin Nutr
53 Suppl 1: S34-43.
Guillet, C., M. Prod'homme, M. Balage, et al. 2004. Impaired anabolic response
of muscle protein synthesis is associated with S6K1 dysregulation in elderly
humans. Faseb J 18(13): 1586-7.
Han, H., R. L. de Vrueh, J. K. Rhie, K. M. Covitz, P. L. Smith, C. P. Lee, D. M.
Oh, W. Sadee and G. L. Amidon (1998). 5'-Amino acid esters of antiviral
nucleosides, acyclovir, and AZT are absorbed by the intestinal PEPT1 peptide
transporter. Pharm Res 15(8): 1154-9.
Han, H. K., D. M. Oh and G. L. Amidon (1998). Cellular uptake mechanism of amino
acid ester prodrugs in Caco-2/hPEPT1 cells overexpressing a human peptide
transporter. Pharm Res 15(9): 1382-6.
Jonas, A. J. and I. J. Butler (1989). Circumvention of defective neutral amino
acid transport in Hartnup disease using tryptophan ethyl ester. J Clin Invest
Kawamura, I., H. Sato, S. Ogoshi, et al. 1985. Use of an intravenous branched
chain amino acid enriched diet in the tumor-bearing rat. Jpn J Surg 15(6):
Kim, D. K., N. Lee, H. T. Kim, G. J. Im and K. H. Kim (1999). Synthesis and
evaluation of 2-amino-6-fluoro-9-(4-hydroxy-3-hydroxymethylbut-1-yl)purine mono-
and diesters as potential prodrugs of penciclovir. Bioorg Med Chem 7(3): 565-70.
Kim, D. K., N. Lee, Y. W. Kim, K. Chang, G. J. Im, W. S. Choi and K. H. Kim
(1999). Synthesis and evaluation of amino acid esters of 6-deoxypenciclovir as
potential prodrugs of penciclovir. Bioorg Med Chem 7(2): 419-24.
Kimball, S. R. and L. S. Jefferson 2006. New functions for amino acids: effects
on gene transcription and translation. Am J Clin Nutr 83(2): 500S-507S.
Kimball, S. R. and L. S. Jefferson 2006. Signaling pathways and molecular
mechanisms through which branched-chain amino acids mediate translational
control of protein synthesis. J Nutr 136(1 Suppl): 227S-31S.
Laviano, A., M. M. Meguid, A. Inui, et al. 2006. Role of leucine in regulating
food intake. Science 313(5791): 1236-8; author reply 1236-8.
Layman, D. K. 2002. Role of leucine in protein metabolism during exercise and
recovery. Can J Appl Physiol 27(6): 646-63.
Layman, D. K. 2003. The role of leucine in weight loss diets and glucose
homeostasis. J Nutr 133(1): 261S-267S.
Lo, H. C. and D. M. Ney 1996. GH and IGF-I differentially increase protein
synthesis in skeletal muscle and jejunum of parenterally fed rats. Am J Physiol
271(5 Pt 1): E872-8.
Lobley, G. E., A. Connell, E. Milne, et al. 1990. Muscle protein synthesis in
response to testosterone administration in wether lambs. Br J Nutr 64(3):
Lynch, C. J. 2001. Role of leucine in the regulation of mTOR by amino acids:
revelations from structure-activity studies. J Nutr 131(3): 861S-865S.
Lynch, C. J., B. Gern, C. Lloyd, et al. 2006. Leucine in food mediates some of
the postprandial rise in plasma leptin concentrations. Am J Physiol Endocrinol
Metab 291(3): E621-30.
Lynch, C. J., B. Halle, H. Fujii, et al. 2003. Potential role of leucine
metabolism in the leucine-signaling pathway involving mTOR. Am J Physiol
Endocrinol Metab 285(4): E854-63.
Lynch, C. J., B. J. Patson, J. Anthony, et al. 2002. Leucine is a direct-acting
nutrient signal that regulates protein synthesis in adipose tissue. Am J Physiol
Endocrinol Metab 283(3): E503-13.
MacLean, D. A., T. E. Graham and B. Saltin 1994. Branched-chain amino acids
augment ammonia metabolism while attenuating protein breakdown during exercise.
Am J Physiol 267(6 Pt 1): E1010-22.
Marchesini, G., R. Marzocchi, M. Noia, et al. 2005. Branched-chain amino acid
supplementation in patients with liver diseases. J Nutr 135(6 Suppl):
Mero, A. 1999. Leucine supplementation and intensive training. Sports Med 27(6):
Mitch, W. E. 1980. Metabolism and metabolic effects of ketoacids. Am J Clin Nutr
Mittleman, K. D., M. R. Ricci and S. P. Bailey 1998. Branched-chain amino acids
prolong exercise during heat stress in men and women. Med Sci Sports Exerc
Mizen, L. and G. Burton (1998). The use of esters as prodrugs for oral delivery
of beta-lactam antibiotics. Pharm Biotechnol 11: 345-65.
Mourier, A., A. X. Bigard, E. de Kerviler, et al. 1997. Combined effects of
caloric restriction and branched-chain amino acid supplementation on body
composition and exercise performance in elite wrestlers. Int J Sports Med 18(1):
Norton, L. E. and D. K. Layman 2006. Leucine regulates translation initiation of
protein synthesis in skeletal muscle after exercise. J Nutr 136(2): 533S-537S.
Ogata, E. S., S. K. Foung and M. A. Holliday 1978. The effects of starvation and
refeeding on muscle protein synthesis and catabolism in the young rat. J Nutr
Okudaira, N., T. Tatebayashi, G. C. Speirs, I. Komiya and Y. Sugiyama (2000). A
study of the intestinal absorption of an ester-type prodrug, ME3229, in rats:
active efflux transport as a cause of poor bioavailability of the active drug. J
Pharmacol Exp Ther 294(2): 580-7.
Petibois, C., G. Cazorla, J. R. Poortmans, et al. 2002. Biochemical aspects of
overtraining in endurance sports: a review. Sports Med 32(13): 867-78.
Platell, C., S. E. Kong, R. McCauley, et al. 2000. Branched-chain amino acids. J
Gastroenterol Hepatol 15(7): 706-17.
Proud, C. G. 2004. Role of mTOR signalling in the control of translation
initiation and elongation by nutrients. Curr Top Microbiol Immunol 279: 215-44.
Proud, C. G., X. Wang, J. V. Patel, et al. 2001. Interplay between insulin and
nutrients in the regulation of translation factors. Biochem Soc Trans 29(Pt 4):
Reeves, J. P. (1979). Accumulation of amino acids by lysosomes incubated with
amino acid methyl esters. J Biol Chem 254(18): 8914-21.
Reeves, J. P. and T. Reames (1981). ATP stimulates amino acid accumulation by
lysosomes incubated with amino acid methyl esters. Evidence for a lysosomal
proton pump. J Biol Chem 256(12): 6047-53.
Rennie, M. J., J. Bohe, K. Smith, et al. 2006. Branched-chain amino acids as
fuels and anabolic signals in human muscle. J Nutr 136(1 Suppl): 264S-8S.
Riazi, R., M. Rafii, L. J. Wykes, et al. 2003. Valine may be the first limiting
branched-chain amino acid in egg protein in men. J Nutr 133(11): 3533-9.
Riazi, R., L. J. Wykes, R. O. Ball, et al. 2003. The total branched-chain amino
acid requirement in young healthy adult men determined by indicator amino acid
oxidation by use of L-[1-13C]phenylalanine. J Nutr 133(5): 1383-9.
Sans, M. D., M. Tashiro, N. L. Vogel, et al. 2006. Leucine activates pancreatic
translational machinery in rats and mice through mTOR independently of CCK and
insulin. J Nutr 136(7): 1792-9.
Sawada, K., T. Terada, H. Saito, Y. Hashimoto and K. I. Inui (1999). Recognition
of L-amino acid ester compounds by rat peptide transporters PEPT1 and PEPT2. J
Pharmacol Exp Ther 291(2): 705-9.
Schliess, F., L. Richter, S. vom Dahl, et al. 2006. Cell hydration and
mTOR-dependent signalling. Acta Physiol (Oxf) 187(1-2): 223-9.
Sherwin, R. S. 1981. The effect of ketone bodies and dietary carbohydrate intake
on protein metabolism. Acta Chir Scand Suppl 507: 30-40.
Shimomura, Y., T. Murakami, N. Nakai, et al. 2000. Suppression of glycogen
consumption during acute exercise by dietary branched-chain amino acids in rats.
J Nutr Sci Vitaminol (Tokyo) 46(2): 71-7.
Silk, D. B., J. E. Hegarty, P. D. Fairclough, et al. 1982. Characterization and
nutritional significance of peptide transport in man. Ann Nutr Metab 26(6):
Sokal, E. M., M. C. Baudoux, E. Collette, et al. 1996. Branched chain amino
acids improve body composition and nitrogen balance in a rat model of extra
hepatic biliary atresia. Pediatr Res 40(1): 66-71.
Stein, T. P., M. R. Donaldson, M. J. Leskiw, et al. 2003. Branched-chain amino
acid supplementation during bed rest: effect on recovery. J Appl Physiol 94(4):
Stipanuk, M. H. 2007. Leucine and protein synthesis: mTOR and beyond. Nutr Rev
Talvas, J., A. Obled, P. Fafournoux, et al. 2006. Regulation of protein
synthesis by leucine starvation involves distinct mechanisms in mouse C2C12
myoblasts and myotubes. J Nutr 136(6): 1466-71.
Tarnopolsky, M. A., S. A. Atkinson, J. D. MacDougall, et al. 1992. Evaluation of
protein requirements for trained strength athletes. J Appl Physiol 73(5):
Tipton, K. D., A. A. Ferrando, S. M. Phillips, et al. 1999. Postexercise net
protein synthesis in human muscle from orally administered amino acids. Am J
Physiol 276(4 Pt 1): E628-34.
Tokunaga, C., K. Yoshino and K. Yonezawa 2004. mTOR integrates amino acid- and
energy-sensing pathways. Biochem Biophys Res Commun 313(2): 443-6.
Wellner, V. P., M. E. Anderson, R. N. Puri, G. L. Jensen and A. Meister (1984).
Radioprotection by glutathione ester: transport of glutathione ester into human
lymphoid cells and fibroblasts. Proc Natl Acad Sci U S A 81(15): 4732-5.
Zhang, Y., K. Guo, R. E. Leblanc, et al. 2007. Increasing dietary leucine intake
reduces diet-induced obesity and improves glucose and cholesterol metabolism in
mice via multi-mechanisms. Diabetes.