N’GAGE AMINO: A Bodybuilding Supplement

More Views

N'GAGE AMINO - 30 Servings

$29.00

Be the first to review this product

$29.00

* Required Fields

$29.00

Details

High Potency INSTANTIZED N’GAGE AMINO

A POWERHOUSE OF AjiPure® BCAA’S SUPERCHARGED WITH Amino-Solve Technology

For N'GAGE AMINO with an Energy Kick, see: N'ERGIZED N'GAGE AMINO

The performance-driving, muscle-building power of BCAAs is now supercharged! Introducing… Instantized N'GAGE Amino – an anabolic powerhouse with exclusive Amino-Sorb Technology. And when we say, "precision," we mean it. You see, unlike "typical" energy and pre-workout and/or recovery products, this dynamic formula is not overloaded with stomach-cramping ingredients.

Therefore, we began the engineering process by formulating exactly opposite of the industry standard. You see, supplemental BCAAs are commonly derived from human hair and bird feathers. That’s pretty disgusting.

Instead, we started with the purest, cleanest form of botanically-derived BCAAs (and L-Glutamine) on the market today. Then, we took these already superior amino acids, instantized them, energized them, and gave them a state-of-the-art flavor profile. This yielded the ultimate, on-the-go, anabolic booster with unprecedented “mixability” and mental ignition, with an unbelievably delicious taste.

But let’s take a brief moment to review the anabolic “nuts and bolts” of this industry-leading formula. Instantized N'GAGE AMINO offers a precise, efficacious dose of four anabolic amino acids: the three Branched Chain Amino Acids and L-Glutamine. Of all the amino acids, these four may offer the most direct impact on energy, growth, recovery and lean muscle preservation.

But we didn’t just use a haphazard, random combo of BCAAs. We aligned this formula with current research for an optimal 2:1:1, L-Leucine-rich ratio to support muscle protein synthesis (packing on slabs of new muscle).

Yep, Instantized N’GAGE AMINO is without question, the absolute benchmark of anabolic-activating, amino acid formulations. It is the standard for which all other BCAA products will be judged. Without a question, any serious, hard-training athlete would be foolish not to incorporate Instantized N’GAGE AMINO into their core supplemental regimen.

By now, you have all the information you need to jump at the chance to try Instantized N’GAGE AMINO. For you techies that want more, read on to get the full scoop on this dynamic formula.

 

QUALITY

 

Of course, nothing but the absolute best amino acids available would do for Axis Labs. That's why all of the amino acids in Instantized N’GAGE AMINO are only ultra premium AjiPure® Amino Acids. Derived exclusively from botanical sources, AjiPure® Amino Acids are instantized for maximum solubility, bioavailability and absorption. This means easy mixing, an amazing taste, no gritty residue, and ultra-fast amino acid availability. AjiPure® represents the very pinnacle of amino acid quality.

 

VERSITILITY

 

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 fueled while supporting recovery. Still, others consume BCAAs first thing in the morning to start "feeding" their hungry muscles.

 

THE POWER OF INSTANTIZED BCAAS (IBCAA)

 

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. However, the BCAAs (and Glutamine) are some of the very first amino acids to be "stripped" from muscle to be used for energy. Therefore, it goes without saying that supplying muscles with BCAAs may have a profound impact on growth and exercise performance. At Axis Labs, we always take the science of performance supplementation to the next level. So, we went back to the proverbial "drawing board" of BCAA research. What we discovered was the incredible power potential of instantized AjiPure®BCAAs. By their very nature BCAAs are readily assimilated into the body. However, in their instantized form, not only are BCAAs more mixable, once ingested they may be launched at hyper-physiological speeds into the bloodstream.

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. That’s why Instantized N’GAGE AMINO features a scientifically validated 2:1:1 L-Leucine-rich BCAA profile. Not only does L-Leucine support protein synthesis (that's muscle growth), it also functions as a trigger for insulin production. Insulin, as you may well know, is a highly anabolic hormone that "delivers" nutrients to tissues; thus supporting performance, growth and recovery.

 

L-GLUTAMINE

 

Glutamine, by far, is the most abundant free amino acid in the body, and in muscle tissue. However, in times of extreme stress, such as intense exercise, the body may not be able to make enough of it. This makes Glutamine a "conditionally essential" amino acid. Therefore, we felt we had an obligation to include a dose of muscle preserving Glutamine in the 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.

 

Amino-Sorb Technology

 

Between the synergy of instantized BCAAs and pharmaceutical-grade AjiPure® Glutamine, N'GAGEhad plenty of body-fueling power.* But we still weren't fully satisfied. We wanted to be certain, beyond the shadow of a doubt, that the Instantized N'GAGE AMINO formulation was fully compliant with our strict standards of perfection. We took the very best amino-acid product on the market and made it even better with exclusive Amino-Sorb Technology™Amino-Sorb Technology™ is a precision blend of bromelain, pyroxidine HCL, and calcium carbonate. It was the exact adjustment we were looking for. Here’s why. Bromelain is a protein-digesting enzyme that may help “chop” proteins and long-chain amino acids into shorter, bioavailable peptides and free form aminos. Piggybacking off of the effects of bromelain is pyroxidine HCL, otherwise known as Vitamin B6. Vitamin B6 helps to metabolize proteins. The combination of bromelain and pyroxidine HCL may help to “supercharge” the bioavailability of other dietary proteins. Completing the Amino-Sorb Technology™ blend is calcium carbonate. This mineral compound may be beneficial in several key ways. First, calcium functions as an electrolyte; it supports bone density, and is involved in muscle contractions. A bonus; the unique form of calcium carbonate may help to temporarily buffer stomach acid.1

 

RESULTS

 

Instantized N'GAGE AMINO is the ideal addition to virtually anyone's supplement regimen. Use it instead of coffee for a delicious, "eye-opening" jolt of pure invigoration. Use a scoop of Instantized N'GAGE AMINO before a workout to help fully engage the body and mind for an intense training session. Try it mid-afternoon for a muscle-fueling, brain-engaging "pick-me-up" at work. College students can leverage the power of Instantized N'GAGE AMINO to help clear the mental "cobwebs" during study. Bottom line, Instantized N'GAGE AMINO is all about fueling individual results.*Instantized N'GAGE AMINO is clearly the only logical choice for anyone seeking a performance boost. It’s delicious, refreshing, and engineered for optimal amino acid performance. What more could you ask for?

Write Your Own Review

You're reviewing: N'GAGE AMINO - 30 Servings

How do you rate this product? *

Rating: 0/5
Vote:

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.

Please wait...

Your product has been added to your shipping cart!
{{var product.name}}