Best BCAA Ethyl Ester – Branched Chain Amino Acids by Axis Labs

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 IGF1
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)

ANABOLIC ACTION

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 anabolic.

ANTI-CATABOLIC

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.

BIOAVAILABILITY

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.
Unknown

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.
Kyle S.

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.
Chris

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.
Adrian, Ireland

Acosta, E. P. and C. V. Fletcher (1997). Valacyclovir. Ann Pharmacother 31(2): 185-91.
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): 1102-6.
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 32(7): 1214-9.
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 63(2): 83-8.
Blomstrand, E., P. Hassmen and E. A. Newsholme 1991. Effect of branched-chain amino acid supplementation on mental performance. Acta Physiol Scand 143(2): 225-6.
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 281(2): E365-74.
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): 798-803.
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): 1-11.
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 84(1): 200-4.
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): 471-6.
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): 691-704.
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): 1596S-601S.
Mero, A. 1999. Leucine supplementation and intensive training. Sports Med 27(6): 347-58.
Mitch, W. E. 1980. Metabolism and metabolic effects of ketoacids. Am J Clin Nutr 33(7): 1642-8.
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 30(1): 83-91.
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): 47-55.
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 108(5): 759-65.
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): 541-7.
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): 337-52.
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): 1345-52.
Stipanuk, M. H. 2007. Leucine and protein synthesis: mTOR and beyond. Nutr Rev 65(3): 122-9.
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): 1986-95.
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.