AllMax MusclEAA EAA's Fruit Punch - 30 Servings *Best by date 10/23

Expiration Date 10/23

MUSCLEAA: EAA SUPPLEMENT

• High EAA Blend With Added BCAAs
• Doubles Muscle Growth
• Doubles Fat Loss
• Get Massive Muscle Pumps
• Boosts Mood
• Amazing Taste

EAA 7 g
MEDIATOR PA 400 mg
SELAGINELLA T 400 mg

MORE MUSCLE, MORE STRENGTH
MUSCLEAA is a full spectrum EAA matrix featuring 7000mg EAAs, including 4200mg BCAAs in a scientifically supported ratio shown to maximize muscle building and fat loss. The inclusion of 400mg Mediator® Phosphatitic Acid and 400mg Selaginella Tamariscina Extract DOUBLES the effectiveness of the EAA matrix.

Why take EAAs?
• Stimulate lean muscle growth and prevent muscle breakdown with the right combination and dose of EAAs. 1, 2, 4, 21
• Helps maintain muscle while restricting calories. 17
• Enhance weight loss as increased protein turnover and muscle mass increases your basal metabolic rate (BMR). 17
• Improve mood as they serve directly as important neurotransmitters or as precursors. 17
• Promote energy production and boost exercise performance. 17

Don’t throw away your BCAAs
BCAAs are important and play crucial roles in our bodies including: activating the enzymes that are responsible for building muscles; regulate blood sugar levels; and decreased recovery time.

Benefits of combining EAAs and BCAAs
• Retain, stimulate and build muscle.
• Enhance mental focus during training.
• Enhance fat burning and glucose tolerance.
• Support hormonal balance during intense training.
• Enhance endurance performance and decrease fatigue.

Stack for faster lean muscle growth and fat loss
To develop a complete physique and improve training performance, we must first be sure that our EAA levels are suitably high. The best way to do this is to take both a reputable EAA product like MUSCLEAA and BCAA formula like AMINOCORE. This, combined with a high protein powder supplement like ISOFLEX, are the keys to building a lean, muscular physique. 19

What are EAAs?

Essential Amino Acids (EAAs) are amino acids that can’t be made by the body – instead are obtained from diet. Diets lacking in amino acids force the body to break down muscle tissue in order to obtain the EAAs needed for other physiological functions. EAAs include: leucine, isoleucine, valine, histidine, lysine, methionine, phenylalanine, threonine, and tryptophan.

How do I take EAAs?

To activate protein synthesis and increase muscle recovery*, take 1 scoop (9.32 g) of MUSCLEAA™ during weight training or any athletic event. On non-training days, MUSCLEAA™ can be taken anytime on an empty stomach. Mix 1 scoop into 17 oz (approx. 500 ml) bottle of water or a tall glass of water (2 cups). Shake or stir well. Take during workouts.

Why should I stack EAAs and BCAAs?

To develop a complete physique and improve training performance, we must first be sure that our EAA levels are suitably high. The best way to do this is to take both a reputable EAA product like MUSCLEAA and  BCAA formula like AMINOCORE. This, combined with a high protein powder supplement like ISOFLEX, are the keys to building a lean, muscular physique.

References

1. Anthony, J. C. et al. (2000). Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation.  Nutr.130, 139–145.
2. Apro, W. et al. (2010). Influence of supplementation with branched-chain amino acids in combination with resistance exercise on p70S6 kinase phosphorylation in resting and exercising human skeletal muscle. Acta Physiol. (Oxf)200, 237–248.
3. Aguiar, A.F. et al. (2017). Free leucine supplementation during an 8-week resistance training program does not increase muscle mass and strength in untrained young adult subjects. Amino Acids. 2017 Jul;49(7):1255-1262.
4. Atherton, P. J. et al. (2010b). Distinct anabolic signalling responses to amino acids in C2C12 skeletal muscle cells. Amino Acids38, 1533–1539.
5. Blomstrand, E. et al. (1997). Influence of ingesting a solution of branched-chain amino acids on perceived exertion during exercise. Acta Physiol Scand. 1997 Jan;159(1):41-9.
6. Escalante, G. et al., The effects of phosphatidic acid supplementation on fitness levels in resistance trained women. Jour Intl Society Sports Nutrn., (2016), 13:24.
7. Hoffman, J. et al., Effects of phosphatidic acid ingestion on lean body mass, muscle thickness and strength gains in resistance-trained men. of the Intl. Society of Sports Nutrn., August 29, 2013.
8. Jackman, S.R. et al. (2017). Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis Following Resistance Exercise in Humans.  Physiol. 8:390.
9. Joy, J. et al., Phosphatidic Acid enhances mTOR signaling and resistance exercise induced hypertrophy. Nutrition & Metabolism, August 1, 2014.
10. Luna-Vázquez, F. J. et al. (2013). Vasodilator compounds derived from plants and their mechanisms of action. Molecules (Basel, Switzerland), 18(5), 5814–5857.
11. Liu, D. et al., Activation of mTORC1 is essential for β–adrenergic stimulation of adipose browning. Clin. Invest. 2016; 126(5):1704-1716.
12. Moberg, M. et al. (2016). Activation of mTORC1 by leucine is potentiated by branched-chain amino acids and even more so by essential amino acids following resistance exercise.  J. Physiol. Cell Physiol.310, C874–C884.
13. Nair, K. S. et al. (1992). Effect of leucine on amino acid and glucose metabolism in humans.  Clin. Exp.41, 643–648.
14. National Center for Biotechnology Information (2020). PubChem Compound Summary for CID 6287, Valine. Retrieved November 22, 2020 from https://pubchem.ncbi.nlm.nih.gov/compound/Valine.
15. National Center for Biotechnology Information (2020). PubChem Compound Summary for CID 6106, Leucine. Retrieved November 22, 2020 from https://pubchem.ncbi.nlm.nih.gov/compound/Leucine.
16. Tipton, K. D. et al. (1999a). Postexercise net protein synthesis in human muscle from orally administered amino acids.  J. Physiol.276, E628–E634.
17. Tessari, P. et al. (2016). Essential amino acids: master regulators of nutrition and environmental footprint?. Scientific reports, 6, 26074.
18. Ward, Z., et al., Projected U.S. State-Level Prevalence of Adult Obesity and Severe Obesity. NEngl J Med 2029: 381:2440- 2450.
19. Witard, O. C. et al. (2014). Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise.  J. Clin. Nutr.99, 86–95.
20. Wiśnik, P. et al. (2011). The effect of branched chain amino acids on psychomotor performance during treadmill exercise of changing intensity simulating a soccer game. Appl Physiol Nutr Metab. 2011 Dec;36(6):856-62.
21. Wu, G. (2009). Amino acids: metabolism, functions, and nutrition. Amino Acids. May;37(1):1-17.
22. Yoon et al. (2017). mTOR as a Key Regulator in Maintaining Skeletal Muscle Mass. Frontiers in Phys, October Vol. 8, Article 788.
23. Kang, D.G. et al. (2004). Vasorelaxation by amentoflavone isolated from Selaginella tamariscina. Planta Med. Aug;70(8):718-22.
24. Suzuki, A. et al. (1999). Properties of amentoflavone, a potent caffeine-like Ca2+ releaser in skeletal muscle sarcoplasmic reticulum. Eur J Pharmacol. May 7;372(1):97-102.
25. Ishola, I.O. et al. (2012). Antidepressant and anxiolytic effects of amentoflavone isolated from Cnestis ferruginea in mice. Pharmacol Biochem Behav. 2012 Dec;103(2):322-31.
26. von Moltke, L.L. et al. (2004). Inhibition of human cytochromes P450 by components of Ginkgo biloba.J Pharm Pharmacol. Aug;56(8):1039-44.