In some cases, you very literally are what you eat. This colloquialism is especially true when you are eating essential amino acids. Amino acids literally form the proteins that make muscle and many other critical components to health and fitness. The 9 essential amino acids can be used to create any of the other 11 dietary amino acids, and the essential amino acids must be consumed in the diet. Amino Prime is made of all 9 EAAs with added glutamine, taurine, and natural caffeine for total workout support.
Instaminos™ branched chain amino acids, leucine, isoleucine, and valine, work to turn on muscle protein synthesis – the recovery process by which we repair and build muscle
Lysine, Threonine, Phenylalanine, Histidine, Methionine, and Tryptophan are the remaining 6 EAAs that supply the muscle with all the building blocks it needs
L-Glutamine supports accelerated recovery, hydration, and glycogen synthesis
L-Taurine support nutrient delivery and exercise capacity
Natural Caffeine boosts natural energy levels
Intense training requires a primed and ready system. Amino Prime was engineered to keep your body ready to push the limit day in and day out. Kick your recovery up a notch with Amino Prime!
Instamino™ Branched Chain Amino Acids
Instamino™ are a specially designed form of amino acids which easily dissolve for a smooth, clean delivery of BCAAs. The BCAAs are unique types of amino acids with a branch-like structure that are especially abundant in muscle.
“turns on” muscle protein synthesis by interacting with the mammalian target of rapamycin (mTOR)
Serves are precursor to anticatabolic metabolites, HMB, HICA, and KIC
Similarly structured to leucine, isoleucine assists with the cellular uptake of leucine, for a more robust anabolic effect
Supports Leucine and Isoleucine functions
May promote glycogen synthesis in muscle cells
Essential Amino Acids
The Essential Amino Acids are required by humans for proper biological function. They cannot be synthesized by the body, and therefore, they must be eaten.
The essential amino acids include the branched chain amino acids, leucine, isoleucine, and valine.
In addition, the EAAs include L-Lysine, L-Threonine, L-Phenylalanine, L-Histidine, L-Methionine, and L-Tryptophan.
These amino acids can be converted to the other 11 dietary amino acids: arginine, alanine, asparagine, aspartate, glycine, glutamate, glutamine, serine, tyrosine, proline, cysteine.
All 20 amino acids are used in the formation of muscle proteins
While being classified as a nonessential amino acid, increased quantities of glutamine may support recovery.
Glutamine can be converted to glucose which can fuel muscle cells and increase glycogen resynthesis
supports the gastrointestinal system by stimulating protein synthesis
May improve hydration
Taurine is a sulfuric amino acid with some specialized effects.
Supports endothelial function
Has antioxidant effects
May improve exercise tolerance and reduce muscle soreness
Caffeine is a xanthine molecule with pronounced biological effects
Caffeine causes adrenaline release
Adrenaline gives us the best of both worlds – increased calorie burn and increased fat burn.
Q: How do I use Amino Prime?
A: As a dietary supplement, mix one scoop of Amino Prime in 8-12 oz of water and drink before, during, and or after training. Amino Prime may also be used to support muscle recovery between meals on training or non-training days. For best results, use 1-2 times daily.
Q: Can I stack any other supplements with Amino Prime?
A: Yes. For the perfect recovery stack, use Amino Prime with Whey Iso. For intense training sessions, use Epitome or Mach-9 pre workout, and drink Amino Prime during the training session.
Branched Chain Amino Acids
Doi, M., Yamaoka, I., Fukunaga, T., & Nakayama, M. (2003). Isoleucine, a potent plasma glucose-lowering amino acid, stimulates glucose uptake in C2C12 myotubes. Biochemical and biophysical research communications, 312(4), 1111-1117.
Doi, M., Yamaoka, I., Nakayama, M., Sugahara, K., & Yoshizawa, F. (2007). Hypoglycemic effect of isoleucine involves increased muscle glucose uptake and whole body glucose oxidation and decreased hepatic gluconeogenesis. American journal of physiology-endocrinology and metabolism, 292(6), E1683-E1693.
Zanchi, N. E., Nicastro, H., & Lancha, A. H. (2008). Potential antiproteolytic effects of L-leucine: observations of in vitro and in vivo studies. Nutrition & metabolism, 5(1), 20.
Drummond, M. J., Fry, C. S., Glynn, E. L., Dreyer, H. C., Dhanani, S., Timmerman, K. L., ... & Rasmussen, B. B. (2009). Rapamycin administration in humans blocks the contraction‐induced increase in skeletal muscle protein synthesis. The Journal of physiology, 587(7), 1535-1546.
Anthony, J. C., Yoshizawa, F., Anthony, T. G., Vary, T. C., Jefferson, L. S., & Kimball, S. R. (2000). Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. The Journal of nutrition, 130(10), 2413-2419.
Blomstrand, E., Hassmén, P., Ek, S., Ekblom, B., & Newsholme, E. A. (1997). Influence of ingesting a solution of branched‐chain amino acids on perceived exertion during exercise. Acta Physiologica Scandinavica, 159(1), 41-49.
Gualano, A. B., Bozza, T., Lopes De Campos, P., Roschel, H., Dos Santos Costa, A., Luiz Marquezi, M., ... & Herbert Lancha Junior, A. (2011). Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. J Sports Med Phys Fitness, 51(1), 82-8.
Essential Amino Acids
Joint, W. H. O. (2007). Protein and amino acid requirements in human nutrition. World health organization technical report series, (935), 1.
Volpi, E., Kobayashi, H., Sheffield-Moore, M., Mittendorfer, B., & Wolfe, R. R. (2003). Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults. The American journal of clinical nutrition, 78(2), 250-258.
Katsanos, C. S., Kobayashi, H., Sheffield-Moore, M., Aarsland, A., & Wolfe, R. R. (2006). A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. American Journal of Physiology-Endocrinology and Metabolism, 291(2), E381-E387.
Bowtell, J. L., Gelly, K., Jackman, M. L., Patel, A., Simeoni, M., & Rennie, M. J. (1999). Effect of oral glutamine on whole body carbohydrate storage during recovery from exhaustive exercise. Journal of Applied Physiology, 86(6), 1770-1777.
Coëffier, M., Claeyssens, S., Hecketsweiler, B., Lavoinne, A., Ducrotté, P., & Déchelotte, P. (2003). Enteral glutamine stimulates protein synthesis and decreases ubiquitin mRNA level in human gut mucosa. American Journal of Physiology-Gastrointestinal and Liver Physiology, 285(2), G266-G273.
Silva, A. C., Santos-Neto, M. S., Soares, A. M., Fonteles, M. C., Guerrant, R. L., & Lima, A. A. (1998). Efficacy of a glutamine-based oral rehydration solution on the electrolyte and water absorption in a rabbit model of secretory diarrhea induced by cholera toxin. Journal of pediatric gastroenterology and nutrition, 26(5), 513-519.
Aruoma, O. I., Halliwell, B., Hoey, B. M., & Butler, J. (1988). The antioxidant action of taurine, hypotaurine and their metabolic precursors. Biochemical Journal, 256(1), 251-255.
Ra, S. G., Miyazaki, T., Ishikura, K., Nagayama, H., Suzuki, T., Maeda, S., ... & Ohmori, H. (2013). Additional effects of taurine on the benefits of BCAA intake for the delayed-onset muscle soreness and muscle damage induced by high-intensity eccentric exercise. In Taurine 8(pp. 179-187). Springer, New York, NY.
Beyranvand, M. R., Khalafi, M. K., Roshan, V. D., Choobineh, S., Parsa, S. A., & Piranfar, M. A. (2011). Effect of taurine supplementation on exercise capacity of patients with heart failure. Journal of cardiology, 57(3), 333-337.
Moloney, M. A., Casey, R. G., O'Donnell, D. H., Fitzgerald, P., Thompson, C., & Bouchier-Hayes, D. J. (2010). Two weeks taurine supplementation reverses endothelial dysfunction in young male type 1 diabetics. Diabetes and Vascular Disease Research, 7(4), 300-310.
Norager, C. B., Jensen, M. B., Weimann, A., & Madsen, M. R. (2006). Metabolic effects of caffeine ingestion and physical work in 75‐year old citizens. A randomized, double‐blind, placebo‐controlled, cross‐over study. Clinical endocrinology, 65(2), 223-228.
Desbrow, B., Biddulph, C., Devlin, B., Grant, G. D., Anoopkumar-Dukie, S., & Leveritt, M. D. (2012). The effects of different doses of caffeine on endurance cycling time trial performance. Journal of sports sciences, 30(2), 115-120.
Mora-Rodríguez, R., Pallarés, J. G., López-Samanes, Á., Ortega, J. F., & Fernández-Elías, V. E. (2012). Caffeine ingestion reverses the circadian rhythm effects on neuromuscular performance in highly resistance-trained men. PLoS One, 7(4), e33807.
Paton, C. D., Lowe, T., & Irvine, A. (2010). Caffeinated chewing gum increases repeated sprint performance and augments increases in testosterone in competitive cyclists. European journal of applied physiology, 110(6), 1243-1250.
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