Protein8 Revolution™

$89.99

ADVANCED 8 SOURCE PROTEIN BLEND*

  • – 30 grams of protein per serving
  • – Fast, medium, & slow digesting proteins
  • – High concentration of naturally occurring BCAAs
  • – Includes IGNITOR™ protein synthesis booster*
  • – 150 calories
  • – Unique & delicious flavors

 

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Description

Nutritionally speaking, having a high protein intake is simply the BEST thing you can do to look and perform better. If you are looking for the ultimate protein for building lean muscle fast, then Protein 8 Revolution is for you. With 30g of protein in the Sustained Release Protein Matrix, you know you’re maximizing your anabolic potential.

Sustained Release Protein Matrix – Whey concentrate, isolate, and peptides elevate amino acids levels quickly, providing a rapid increase in muscle protein synthesis, while milk protein isolate and micellar casein extend anabolism for hours!

Anticatabolic Amino Blend – Additional branched-chain amino acids, glutamine, taurine, and glycine provide additional muscle fuels, stimulate growth, enhance protein absorption, and help with amino acid conjugation.

IGNITOR™ Amino Releasing Matrix – A proprietary blend of proteolytic enzymes designed and optimized to efficiently release branch chain amino acids (BCAAs) and glutamine from whey protein sources while promoting heightened mTOR activation for enhanced protein synthesis and skeletal muscle growth.

You put a lot into your training, and to recover, you need a quality protein. Make sure that your protein is working as hard as you are. Protein 8 Revolution will not only bolster the effects of your training regimen, but it will allow you to go harder week-in and week-out!

*These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease.

Supplement Facts

*Nutritional information may vary slightly between flavors

Ingredient Profile

Sustained Release Protein Matrix

Whey Protein as a whole:

Proteins provide the building blocks of muscle via their constituent amino acids.  However, quality, digestion rate, and source should be considered when selecting a protein. In general, the essential amino acid content determines the quality of the protein. In particular, two to three grams of leucine is needed to optimize protein synthesis. Whey contains 11% leucine making it one of the highest quality proteins available. Whey is also very water soluble, mixes easily, and digests rapidly which is important for stimulating muscle protein synthesis after a hard training session.  After ingestion of whey, amino acids levels in the blood are elevated after 1.5 hours and return to baseline after ~5 hours.  This is why it is recommended to consume protein (25-30 grams optimally) every 3-4 hours when trying to build muscle; to keep amino acids levels in the blood elevated which will continue muscle protein synthesis and help promote recovery and repair of damaged muscle tissue.

Whey (milk based) proteins may also have positive effects on glycogen replenishment following exercise. Research has demonstrated that the addition of protein to a moderate carbohydrate beverage may speed glycogen replenishment following a hard training session.  Since glycogen is used to provide a significant amount of the energy needs during intense training it is important to have stores replenished in order to meet the needs of subsequent training sessions.

Lastly milk based proteins have many significant health benefits that many tend to overlook. For example, lactalbumin, a peptide found in whey may appears to play a role in enhancing lymphatic and immune system responses, may enhance cognitive function, improve sleep, and has many antibacterial, antiviral, and antioxidant properties.

Potential Benefits:

  • Promotes muscle protein synthesis
  • Digests and absorbs quickly
  • Increases lean mass
  • Increase power and strength via the increase in muscle size
  • Speeds recovery from muscle damaging exercises
  • Increases glycogen replenishment
  • Contains highest amount of leucine compared to other sources
  • May decrease body weight gain


Whey Protein Concentrate:

Whey protein concentrate is the most common form of whey, a byproduct formed when acid is added to milk.

  • Whey protein concentrate is the closest to whole food compared to other forms of protein and is 75-85% pure protein after filtration.
  • A growing body of evidence suggests that dairy protein, and whey in particular may: 1) stimulate the greatest rise in muscle protein synthesis, 2) result in greater muscle cross-sectional area when combined with chronic resistance training, and 3) at least in younger individuals, enhance exercise recovery.


Calcium Caseinate:

Calcium Caseinate contains approximately 90% protein whilst also being a rich source of minerals and amino acids such as Glutamine.

  • Calcium Caseinate is digested very slowly by the body therefore it can be used before bed as you slowly absorb amino acids to keep your body in an anabolic state when you sleep.
  • It can also be used when you have a long time between meals to provide you with a source of protein and to keep you feeling full.
  • Calcium Caseinate differs from Micellar Casein in the way in which it is more soluble. Calcium Caseinate is formed when an alkaline substance (Calcium) is reacted with the casein. This helps to raise the mineral content of this form of casein.


Milk Protein Isolate:

Milk protein isolate is 20% whey protein and 80% micellar casein.

  • This ratio in beneficial due to the whey digesting and absorbing rapidly, while the casein digests and absorbs more slowly.
  • This leads to longer muscle protein synthesis times.


Whey Protein Isolate:

Whey protein isolates digest and absorb rapidly and are, gram for gram, the most refined and purest form of protein (90-98% pure protein).

  • It is also a potent stimulator of muscle protein synthesis due to its ability to causes a rapid increase in amino acids found in the blood stream.
  • This form of whey contains little to no lactose so it may be beneficial for individuals who experience GI problems. Also due to the refinement process whey isolate contains little fat, carbs, and milk sugars.
  • A 2006 study conducted by Cribb et al. found recreational bodybuilders who supplemented with whey protein isolate in conjunction with a 10 week resistance training program achieved greater gains in lean mass, strength, and decreases in body fat compared to a placebo group.


Beef Protein Isolate:

Beef protein with over 98% of pure proteins. Easy to digest, high on essential amino acids and low on calories.


Whey Protein Peptides:

Whey protein peptides are pre-digested proteins (broken down into amino acids).

  • This breakdown leads to faster absorption by the body thus rapidly rebuilding and repairing muscles after a workout.


Micellar Casein:

Casein is a phosphoprotein largely found in dairy products like milk and cheese.

  • Casein protein does not have as much of an anabolic effect as whey because it is not absorbed as quickly.
  • However, the rate of protein synthesis for whey protein drops after a few hours whereas it remains consistent with casein.
  • This characteristic is most helpful in preventing the onset of catabolism.
  • Recent research confirms that combining fast-digesting whey protein with slow-digesting casein protein is better for muscle growth than just going with whey protein alone.


Egg Protein:

Egg protein is easily digested, absorbed, and tolerated by most individuals.  Egg albumin is high in BCAAs and arginine, contributing to hormone production and muscle building.


Anticatabolic Amino Blend

Glycine:

Glycine is a non-essential amino acid that is used to help generate muscle tissue, assist with proper cell growth and production, and convert glycogen into energy. It also plays an important role in proper nervous system function.

  • Glycine is required for the biosynthesis of creatine. Glycine increases the body’s creatine levels and helps prevent the breakdown of muscle.
  • In the absence of glycine, damaged muscle tissue cannot be repaired.
  • Current research has suggested that glycine supplementation may increase growth hormone (GH) levels 3-4 hours post exercise via its stimulatory agents acting upon the pituitary gland. This increase in GH theoretically could lead to faster recovery times and greater muscle growth.

L-Glutamine:

L-glutamine is the most prevalent free amino acid in plasma and one of the most prevalent found in muscle tissue.

  • L-Glutamine stimulates muscle protein synthesis and is effective at replenishing energy for muscles (glycogen) after exhaustive exercise which may lead to quicker recovery.
  • L-Glutamine may also increase cell volumization (hydration) and lead to increases in muscle hypertrophy.
  • L-Glutamine may also reduce protein breakdown and support immune function.
  • Lehmkuhl et al. (2003) found individual supplementing with glutamine and creatine monohydrate for 8 weeks increased body mass, lean body mass and initial rate of power production compared to placebo.

BCAAs (Leucine, Isoleucine, Valine):

The essential amino acids Leucine, Isoleucine, and Valine collectively form what is referred to as the Branched Chain Amino Acids (BCAAs). These amino acids are essential because they cannot be produced in the body and must be provided though supplementation or diet. BCAAs comprise approximately 30% of the total muscle protein pool and are the primary amino acids oxidized in the muscle during exercise and catabolic stress.  For these reasons athletes supplement with BCAAs for the purpose of increasing muscle mass, reducing muscle damage, blunting fatigue, and increasing energy during exercise.

  • Hundreds of studies exist on the ergogenic benefits of BCAAs.  The majority of them show that BCAAs, whether consumed pre, during, or post-exercise; decrease protein catabolism (breakdown) and support muscle protein synthesis…a physiological process responsible for muscle growth and repair.  Furthermore, BCAAs are vitally important to glucose (energy) production; contributing to greater than 40% of glucose production during sustained endurance exercise.
  • A study done in 2009 found that subjects who supplemented with BCAAs while following an 8-week resistance training program had a greater decrease in body fat, an increase in lean mass, and greater strength gains on the bench press and squat compared to the non-BCAA group.

Tauric Acid:

Taurine has a myriad of benefits. From helping the body to metabolize fat, improving insulin sensitivity, raising testosterone levels, as an antioxidant, higher performance and quicker recovery during athletic training and increasing cardiovascular health… it goes without saying that taurine is a great ingredient to have in your wheelhouse

  • Zhang et al. (2004) found that individuals who supplemented with taurine for 1 week before an exhaustive exercise bout significantly improved time to exhaustion, VO2 max, and maximal workload. It also decreased exercise induced DNA damage
FAQs

Q: What is the best way to take Protein 8 Revolution?
A: Take 1 serving (1 Scoop) of Protein 8 Revolution with 12-16 oz of cold water or any beverage of your choice. For optimal flavor & a smoothie consistency, mix in a blender with ice.

Q: When is the best time to take Protein 8 Revolution?
A: We suggest consuming one serving Immediately post workout when your body is in need of critical nutrients to maximize muscle protein synthesis; which ultimately leads to muscular growth and recovery. It can also be consumed between meals to meet daily protein requirements.

Q: Is consuming too much protein bad for your kidneys?
A: Absolutely not. This is a myth. No piece of scientific literature exists showing that eating a high protein diet has any detrimental effects on renal function in otherwise healthy individuals.

Q: Can’t I meet my daily protein requirements through a regular diet?
A: While it is possible to meet daily protein requirements through a balanced diet; some individuals find it difficult to get the 1.5 -2 grams per kg/bodyweight necessary to maximize muscle growth and promote recovery. This is why individuals often turn to whey protein supplementation as a convenient way to meet their individual protein needs.

Q: What other MuscleSport products do you recommend stacking with Protein 8 Revolution?
A: To create the most anabolic environment for muscle growth and recovery we recommend stacking Protein 8 Revolution with one of our creatine products and Test Revolution.

References

Whey Protein as a whole:
1. Campbell, B., Kreider, R. B., Ziegenfuss, T., La Bounty, P., Roberts, M., Burke, D., … & Antonio, J. (2007). Journal of the International Society of Sports Nutrition. Journal of the International Society of Sports Nutrition, 4(8), 8.
2. Antonio, J., & Stout, J. R. (2001). Sports supplements. Lippincott Williams & Wilkins.
3. Smith-Ryan, A., & Antonio, J. (Eds.). (2013). Sports Nutrition & Performance Enhancing Supplements. Linus Learning.
4. Lemon, P. W. (1991). Protein and amino acid needs of the strength athlete. Int J Sport Nutr, 1(2), 127-145.
5. Zawadzki, K. M., Yaspelkis, B. B. D., & Ivy, J. L. (1992). Carbohydrate-protein complex increases the rate of muscle glycogen storage after exercise. Journal of Applied Physiology, 72(5), 1854-1859.
6. Markus, C. R., Olivier, B., & de Haan, E. H. (2002). Whey protein rich in α-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. The American journal of clinical nutrition, 75(6), 1051-1056.
7. Cockburn, E., Stevenson, E., Hayes, P. R., Robson-Ansley, P., & Howatson, G. (2010). Effect of milk-based carbohydrate-protein supplement timing on the attenuation of exercise-induced muscle damage. Applied Physiology, Nutrition, and Metabolism, 35(3), 270-277.
8. Wojcik, J. R., Walber-Rankin, J., Smith, L. L., & Gwazdauskas, F. C. (2001). Comparison of carbohydrate and milk-based beverages on muscle damage and glycogen following exercise. International journal of sport nutrition and exercise metabolism, 11(4), 406-419.
9. Belobrajdic, D. P., McIntosh, G. H., & Owens, J. A. (2004). A high-whey-protein diet reduces body weight gain and alters insulin sensitivity relative to red meat in wistar rats. The Journal of nutrition, 134(6), 1454-1458.

Whey Protein Concentrate:
1. Hulmi, J. J., Lockwood, C. M., & Stout, J. R. (2010). Effect of protein/essential amino acids and resistance training on skeletal muscle hypertrophy: A case for whey protein. Nutrition & metabolism, 7(1), 1.
2. Hoffman, J. R., & Falvo, M. J. (2004). Protein-Which is best. Journal of Sports Science and Medicine, 3(3), 118-130.
3. Hayes, A., & Cribb, P. J. (2008). Effect of whey protein isolate on strength, body composition and muscle hypertrophy during resistance training. Current Opinion in Clinical Nutrition & Metabolic Care, 11(1), 40-44.
4. Volek, J. S., Volk, B. M., Gómez, A. L., Kunces, L. J., Kupchak, B. R., Freidenreich, D. J., … & Quann, E. E. (2013). Whey protein supplementation during resistance training augments lean body mass. Journal of the American College of Nutrition, 32(2), 122-135.
5. Renan, M., Mekmene, O., Famelart, M. H., Guyomarc’h, F., Arnoult-Delest, V., Pâquet, D., & Brulé, G. (2006). pH-Dependent behaviour of soluble protein aggregates formed during heat-treatment of milk at pH 6· 5 or 7· 2. Journal of dairy research, 73(01), 79-86.

Whey Protein Isolate:
1. Hayes, A., & Cribb, P. J. (2008). Effect of whey protein isolate on strength, body composition and muscle hypertrophy during resistance training. Current Opinion in Clinical Nutrition & Metabolic Care, 11(1), 40-44.
2. Pal, S., Ellis, V., & Dhaliwal, S. (2010). Effects of whey protein isolate on body composition, lipids, insulin and glucose in overweight and obese individuals. British journal of nutrition, 104(05), 716-723.
3. Burd, N. A., Yang, Y., Moore, D. R., Tang, J. E., Tarnopolsky, M. A., & Phillips, S. M. (2012). Greater stimulation of myofibrillar protein synthesis with ingestion of whey protein isolate v. micellar casein at rest and after resistance exercise in elderly men. British Journal of nutrition, 108(06), 958-962.
4. Cooke, M. B., Rybalka, E., Stathis, C. G., Cribb, P. J., & Hayes, A. (2010). Whey protein isolate attenuates strength decline after eccentrically-induced muscle damage in healthy individuals. J Int Soc Sports Nutr, 7(1), 30.
5. Renan, M., Mekmene, O., Famelart, M. H., Guyomarc’h, F., Arnoult-Delest, V., Pâquet, D., & Brulé, G. (2006). pH-Dependent behaviour of soluble protein aggregates formed during heat-treatment of milk at pH 6· 5 or 7· 2. Journal of dairy research, 73(01), 79-86.
6. Whetstine, M. C., Croissant, A. E., & Drake, M. A. (2005). Characterization of dried whey protein concentrate and isolate flavor. Journal of dairy science,88(11), 3826-3839.

Whey Protein Peptides:
1. Farup, J., Rahbek, S. K., Vendelbo, M. H., Matzon, A., Hindhede, J., Bejder, A., … & Vissing, K. (2014). Whey protein hydrolysate augments tendon and muscle hypertrophy independent of resistance exercise contraction mode. Scandinavian journal of medicine & science in sports, 24(5), 788-798.
2. Calbet, J. A., & MacLean, D. A. (2002). Plasma glucagon and insulin responses depend on the rate of appearance of amino acids after ingestion of different protein solutions in humans. The Journal of nutrition, 132(8), 2174-2182.
3. Calbet, J. A., & Holst, J. J. (2004). Gastric emptying, gastric secretion and enterogastrone response after administration of milk proteins or their peptide hydrolysates in humans. European journal of nutrition, 43(3), 127-139.
4. Buckley, J. D., Thomson, R. L., Coates, A. M., Howe, P. R., DeNichilo, M. O., & Rowney, M. K. (2010). Supplementation with a whey protein hydrolysate enhances recovery of muscle force-generating capacity following eccentric exercise. Journal of Science and Medicine in Sport, 13(1), 178-181.

Milk Protein Isolate:
1. Boirie, Y., et al. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc. Natl. Acad. Sci. USA 94:14930–14935, 1997.
2. Reidy, P. T., et al. Protein Blend Ingestion Following Resistance Exercise Promotes Human Muscle Protein Synthesis. J Nutr. 143(4):410-416, 2013.
3. Soop, M., et al. Coingestion of whey protein and casein in a mixed meal: demonstration of a more sustained anabolic effect of casein. Am J Physiol Endocrinol Metab. 2012 Jul 1;303(1):E152-62.
4. Kerksick, CM, et al. The effect of protein and amino acid supplementation in performance and training adaptations during ten weeks of resistance training. Journal of Strength and Conditioning Research 20(3), 643–653, 2006.
5. Paul, G. L., et al. The rationale for consuming protein blends in sports nutrition. Journal of the American College of Nutrition 28 (4):464S–472S, 2009.
6. Tipton KD, Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Med Sci Sports Exerc. 2004 Dec;36(12):2073-81.

Micellar Casein:
1. Tipton, K. D., Elliott, T. A., Cree, M. G., Wolf, S. E., Sanford, A. P., & Wolfe, R. R. (2004). Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Medicine and Science in Sports and Exercise, 36, 2073-2081.
2. Tang, J. E., Moore, D. R., Kujbida, G. W., Tarnopolsky, M. A., & Phillips, S. M. (2009). Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. Journal of Applied Physiology, 107(3), 987-992.
3. Snijders, T., Smeets, J. S., van Vliet, S., van Kranenburg, J., Maase, K., Kies, A. K., … & van Loon, L. J. (2015). Protein ingestion before sleep increases muscle mass and strength gains during prolonged resistance-type exercise training in healthy young men. The Journal of nutrition, 145(6), 1178-1184.

Glycine:
1. Wax, B., Hilton, L., Vickers, B., Gilliland, K., & Conrad, M. (2013). Effects of glycine-arginine-alpha-ketoisocaproic acid supplementation in college-age trained females during multi-bouts of resistance exercise. J Diet Suppl, 10(1), 6-16.
2. Nelson, M. J., Harris, M. B., Boluyt, M. O., Hwang, H. S., & Starnes, J. W. (2011). Effect of N-2-mercaptopropionyl glycine on exercise-induced cardiac adaptations. [Research Support, Non-U.S. Gov’t]. Am J Physiol Regul Integr Comp Physiol, 300(4), R993-R1000..
3. Jacobs, P. L., & Goldstein, E. R. (2010). Long-term glycine propionyl-l-carnitine supplemention and paradoxical effects on repeated anaerobic sprint performance. J Int Soc Sports Nutr, 7, 35. doi: 10.1186/1550-2783-7-35
4. Bloomer, R. J., Tschume, L. C., & Smith, W. A. (2009). Glycine propionyl-L-carnitine modulates lipid peroxidation and nitric oxide in human subjects. [Randomized Controlled Trial Research Support, Non-U.S. Gov’t]. Int J Vitam Nutr Res, 79(3), 131-141.
5. Jacobs, P. L., Goldstein, E. R., Blackburn, W., Orem, I., & Hughes, J. J. (2009). Glycine propionyl-L-carnitine produces enhanced anaerobic work capacity with reduced lactate accumulation in resistance trained males. J Int Soc Sports Nutr, 6, 9. doi: 10.1186/1550-2783-6-9

L-Glutamine:
1. Welbourne, T. C. (1995). “Increased plasma bicarbonate and growth hormone after an oral glutamine load”. The American journal of clinical nutrition 61 (5): 1058–1061.
2. Morlion, B. J.; Stehle, P.; Wachtler, P.; Siedhoff, H. P.; Köller, M.; König, W.; Fürst, P.; Puchstein, C. (1998). “Total Parenteral Nutrition with Glutamine Dipeptide After Major Abdominal Surgery”. Annals of Surgery 227 (2): 302–308.
3. Lee, W. J.; Hawkins, R. A.; Viña, J. R.; Peterson, D. R. (1998). “Glutamine transport by the blood-brain barrier: A possible mechanism for nitrogen removal”. The American journal of physiology 274
4. Todorova, V. K., Kaufmann, Y., Luo, S., & Klimberg, V. S. (2011). Tamoxifen and raloxifene suppress the proliferation of estrogen receptor-negative cells through inhibition of glutamine uptake. [Research Support, U.S. Gov’t, Non-P.H.S.]. Cancer Chemother Pharmacol, 67(2), 285-291.
5. 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.

BCAAs:
1. Norton, L. E., & Layman, D. K. (2006). Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. The Journal of nutrition, 136(2), 533S-537S.
2. Shimomura, Y., Inaguma, A., Watanabe, S., Yamamoto, Y., Muramatsu, Y., Bajotto, G., … & Mawatari, K. (2010). Branched-chain amino acid supplementation before squat exercise and delayed-onset muscle soreness. International journal of sport nutrition, 20(3), 236.
3. Gualano, A. B., Bozza, T., Lopes, D. C. P., Roschel, H., Dos Santos, C. A., Luiz, M. M., … & Herbert, L. J. A. (2011). Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. The Journal of sports medicine and physical fitness, 51(1), 82-88.
4. Hamel, F. G., Upward, J. L., Siford, G. L., & Duckworth, W. C. (2003). Inhibition of proteasome activity by selected amino acids. Metabolism, 52(7), 805-809.
5. Nicastro, H., Artioli, G. G., dos Santos Costa, A., Solis, M. Y., Da Luz, C. R., Blachier, F., & Lancha Jr, A. H. (2011). An overview of the therapeutic effects of leucine supplementation on skeletal muscle under atrophic conditions. Amino Acids, 40(2), 287-300.
6. 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.
7. Stoppani, J., Scheett, T. P., Pena, J., Rudolph, C., Charlebois, D., & Charleston, S. C. (2009). Consuming branched-chain amino acid supplement during a resistance training program increases lean mass, muscle strength and fat loss. Journal of the International Society of Sports Nutrition, 6(Suppl 1), P1.

Taurine:
1. Zhang, M., Izumi, I., Kagamimori, S., Sokejima, S., Yamagami, T., Liu, Z., & Qi, B. (2004). Role of taurine supplementation to prevent exercise-induced oxidative stress in healthy young men. Amino acids, 26(2), 203-207.
2. BOUCHAMA, A., YUSUF, A., AL-SEDAIRY, S. U. L. T. A. N., & EL-YAZIGI, A. D. N. A. N. (1993). Alteration of taurine homeostasis in acute heatstroke.Critical care medicine, 21(4), 551-554.
3. Gwacham, N., & Wagner, D. R. (2012). Acute effects of a caffeine-taurine energy drink on repeated sprint performance of American college football players. Int J Sport Nutr Exerc Metab, 22(2), 109-116.
4. Warskulat, U., Brookmann, S., Felsner, I., Brenden, H., Grether‐Beck, S., & Häussinger, D. (2008). Ultraviolet A induces transport of compatible organic osmolytes in human dermal fibroblasts. Experimental dermatology, 17(12), 1031-1036.

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