N'ERGIZED AMINO Supplement with INSTANTIZED BCAA'S
UNLOCK THE TRUE POWER OF AjiPure® BCAA’S WITH AMINO-SOLVE + INVIGORATION
5g iBCAA + 2.5g Glutamine AjiPure Aminos Mixes Instantly Tastes Great No Dyes
N’ERGIZED AMINO The performance-driving, muscle-building power of BCAAs is now supercharged! Introducing, N’Ergized Amino Instantized BCAAs - a powerhouse of precision formulation. And when we say, "precision," we mean it. You see, unlike "typical" energy and pre-workout products, this dynamic formula is not bogged down by ingredient overload. We are definitely not interested in "wowing" you with a long supplement facts panel. We'll leave that strategy for the "other guys." Instead, we are interested in getting you results. N’ergized Instantized BCAAs offers a precise, efficacious dose of four anabolic amino acids: the three Branched Chain Amino Acids and L-Glutamine.* Why just these four? Of all the amino acids, these four may offer the most direct impact on supporting growth, recovery and lean muscle preservation.* Now, we could have included a few more of the essential amino acids into the mix (like other products), but we just didn't see the need. Why would we add more types of amino acids into the formula when we could just add higher amounts of the ones that really matter? Remember, this is a precision formula.
Of course, nothing but the absolute best amino acids available would do for this product. After all, we're Axis Labs. You can count on us to formulate with premium grade ingredients. That's why all of the amino acids in INSTANTIZED N’Ergized Amino are only ultra premium AjiPure® Amino Acids - the pinnacle of quality. Derived exclusively from botanical sources, AjiPure® Amino Acids are instantized for maximum solubility, bioavailability and absorption.* For you, this means easy mixing, a super clean taste, no gritty residue, and ultra-fast amino acid availability.*
The question that may still be burning in your mind is, "Why incorporate caffeine into a BCAA formula?" The answer is quite simple, really. We developed N’Ergized INSTANTIZED Amino to deliver pure performance.* Now, let's define "performance." Performance is a term most often associated with physical performance. However, there is such a thing as "mental performance." Incidentally, physical performance and mental performance are not independent. For example, it is difficult to achieve a great workout if you are not focused. Likewise, staying focused during a workout is difficult when your body is sore from the last training session.*
Caffeine is a naturally-occurring compound that offers three invigorating benefits.* First, caffeine is well noted for its role in supporting focus and mental acuity.* Second, caffeine is associated with influencing lipolysis - the breakdown of stored fats for use as fuel.* Third, caffeine supports strong muscle contractions through "mind-muscle" connections.* These powerful factors make caffeine and the Branched Chain Amino Acids a perfect match for a wide range of scenarios. For example, many athletes use BCAAs prior to a training session to support energy production and lean muscle protection.* Regular users of BCAAs report that a mid-afternoon serving helps them to stay energized while supporting recovery.* Still, others consume BCAAs first thing in the morning to start "feeding" their hungry muscles.* In each of these examples, the mind and muscle-supporting attributes of caffeine offers a complimentary host of benefits.*
INSTANTIZED N’Ergized Amino is the ideal addition to virtually anyone's supplement regimen. Use Instantized N’Ergized INSTANTIZED Amino instead of coffee for a delicious, "eye-opening" jolt of invigorating muscle support.* Use a scoop of INSTANTIZED N’Ergized Amino before a workout to help fully engage the body and mind for an intense training session.* Use mid-afternoon for a muscle-fueling "pick-me-up."* When you need something to clear the mental "cobwebs" at work, try a scoop of INSTANTIZED N’Ergized Amino for support.* Bottom line, INSTANTIZED N’Ergized Amino is all about fueling results.*
A GUIDE TO BCAAS
For years, the BCAAs have been hailed as having a unique capacity to support performance, recovery and growth…and for good reason.* Human muscle is comprised of a specific sequence and ratio of essential amino acids (EAAs), a substantial portion of that ratio being the BCAAs: L-Leucine, L-Isoleucine and L-Valine. Now, intense exercise and sport requires volumes of readily available fuel to power muscles.* As the body's "standard" energy reserves become depleted, it may begin converting amino acids into useable fuel. Here is where things get interesting. The BCAAs (and Glutamine) are some of the very first amino acids to be "stripped" from muscle to be used for energy.* Now, since such a large portion of muscle protein is comprised of the BCAAs, and because the BCAAs are the first to be "pulled" from muscle during exercise, it goes without saying that re-supplying damaged muscles with BCAAs post-exercise has profound, growth and performance-specific support implications.*
THE POWER OF INSTANTIZED BCAAS (IBCAA)
At Axis Labs, we always take the science of performance supplementation to the next level. You see, we simply could have just formulated a standard BCAA product and launched it as something "new and exciting." However, our integrity and pride for excellence continually guide our every move. As such, we tasked ourselves to develop a truly unique BCAA supplement. So, we went back to the proverbial "drawing board" of BCAA research. What we found was "instantized" AjiPure® BCAAs. This was groundbreaking news. You see the BCAAs are, by nature, are rapidly assimilated into the body. However, through instantizing technology, BCAAs may be launched at hyper-physiological speeds to hungry muscles.* Simply put, ultra-fast absorption of BCAAs offers the potential for them to support performance, growth and recovery faster, and more efficiently than previously possible.*
THE 2:1:1 FACTOR
Although all three of the BCAAs are highly important, one of them stands apart as a growth-inducing juggernaut*; L-Leucine. L-Leucine triggers an array of "downstream" metabolic pathways that directly and indirectly support performance.* For example, not only does L-Leucine support protein synthesis (that's muscle growth), it also functions as a trigger for insulin production and release.* Insulin, as you may well know, is a highly anabolic hormone that "delivers" nutrients to tissues; thus supporting performance, growth and recovery.* In order to take full advantage of the power of L-Leucine, we formulated INSTANTIZED N’Ergized Amino with a 2:1:1 ratio (L-Leucine: L-Isoleucine: L-Valine).
Glutamine, by far, is the most abundant free amino acid in the body, and in muscle tissue. Furthermore, Glutamine is used in a broad range of physiological processes that are not necessarily "bodybuilding" related.* In fact, much of naturally produced Glutamine may be quickly "ravaged" by the body before it even has a chance to go to work in muscles. This makes Glutamine a "conditionally essential" amino acid for tissue repair. In other words, in times when your body can't make enough of its own Glutamine to sustain all of its needs, it "becomes" essential.* Therefore, supplemental Glutamine may be incredibly beneficial. So, we obviously had an obligation to include a dose of Glutamine in our new formulation. True to our nature, we didn't just go with just "any old" Glutamine—that is not the Axis Labs way. We chose the very best source of Glutamine we could find—AjiPure® Glutamine, to be specific. AjiPure® Glutamine is a premium, pharmaceutical-grade product produced under stringent cGMP manufacturing regulations.
INSTANTIZED N’Ergized Amino is clearly the only logical choice for serious athletes. It’s delicious, refreshing, and engineered for optimal amino acid performance.
References: 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. 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. 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 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. 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. 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. 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. 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. 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. 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. 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. 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.