$59.99
Meat-Free

Wild Caught Marine Collagen Peptides Powder.

$59.99
New Arrival
Codeage Wild-Caught Marine Collagen powder supplement offers hydrolyzed collagen of types 1 & 3, sustainably sourced from North American ocean white fish. Packed with 18 amino acids, this pure fish collagen powder supplement is also ideal for those seeking a meatless collagen supplement.
Codeage Wild-Caught Marine Collagen powder supplement offers hydrolyzed collagen of types 1 & 3, sustainably sourced from North American ocean white fish. Packed with 18 amino acids, this pure fish collagen powder supplement is also ideal for those seeking a meatless collagen supplement.

SUGGESTED USE.

Adults, 1 scoop 1 time per day. Mix one scoop in 8-10 ounces of your favorite beverage once each day. Collagen can also be sprinkled over food. Take at least one hour prior to or after taking medication or natural health products.

SEE CAUTION

CAUTION: Keep out of the reach of children. Consult a health care practitioner/health care provider/health care professional/doctor/physician prior to use if you are pregnant or breastfeeding. Known Adverse Reactions: May cause mild gastrointestinal disturbances. Precautions for Use: Store in a cool, dry place. Store in airtight container, protected from light, heat and moisture. Do not use if product has been opened or tampered with in any way.

ADDITIONAL DETAILS.

Pure and Wild-Caught Fish Collagen Powder

Pure superiority.

Purity and quality are paramount. Each product captures genuine, authentic essence from prime sources to ensure unmatched excellence.

Global ingredients.

Superior elements represent the pinnacle of nutritional excellence and are celebrated for their elevatednutritional profiles.

Modern approach.

Manufactured with global ingredients and blended using state-of-the-art equipment to uphold the highest standards of integrity.

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Product Details

  • Codeage Wild-Caught Marine Collagen supplement is sustainably sourced from deep-ocean white fish in North American cold waters, providing a high concentration of type 1 & 3 collagen in a convenient powder format.
  • This marine collagen powder supplement delivers 18 essential and non-essential amino acids, offering comprehensive support to your overall health and well-being.*
  • This pure fish collagen supplement formula is uncompromising in its purity. This marine collagen peptides supplement is non-GMO, dairy-free, and gluten-free. This hydrolyzed fish collagen contains zero carbs, with no additives, preservatives, or sulfites, making it a clean and wholesome addition to your daily routine. This meatless collagen is also shellfish-free.
  • This versatile hydrolyzed collagen powder formula allows you to mix it into beverages, protein shakes, or your favorite recipes.
  • Codeage Wild-Caught Marine Collagen powder is manufactured in the USA with global ingredients in a cGMP-certified facility for quality and purity.

Supplement Facts

Supplement Facts

Ingredients

Medicinal Ingredients (per scoop [approximately 9 g]): Hydrolyzed collagen (Fish - skin) 9 g. Non-Medicinal Ingredients: None.

Packaged by weight, not volume. Settling may occur.

Suggested Use

Adults, 1 scoop 1 time per day. Mix one scoop in 8-10 ounces of your favorite beverage once each day. Collagen can also be sprinkled over food. Take at least one hour prior to or after taking medication or natural health products.

CAUTION: Keep out of the reach of children. Consult a health care practitioner/health care provider/health care professional/doctor/physician prior to use if you are pregnant or breastfeeding. Known Adverse Reactions: May cause mild gastrointestinal disturbances. Precautions for Use: Store in a cool, dry place. Store in airtight container, protected from light, heat and moisture. Do not use if product has been opened or tampered with in any way.

References

Wild Caught Hydrolyzed Fish Collagen

Sanchez A, Blanco M, Correa B, Perez-Martin RI, Sotelo CG. Effect of Fish Collagen Hydrolysates on Type I Collagen mRNA Levels of Human Dermal Fibroblast Culture. Mar Drugs. 2018;16(5):144. Published 2018 Apr 26. doi: 10.3390/md16050144

König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women-A Randomized Controlled Study. Nutrients. 2018;10(1):97. Published 2018 Jan 16. doi: 10.3390/nu10010097

Porfírio, Elisângela & Fanaro, Gustavo. (2016). Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: a systematic review. Revista Brasileira de Geriatria e Gerontologia. 19. 153-164. DOI: 10.1590/1809-9823.2016.14145

De Luca C, Mikhal'chik EV, Suprun MV, Papacharalambous M, Truhanov AI, Korkina LG. Skin Antiageing and Systemic Redox Effects of Supplementation with Marine Collagen Peptides and Plant-Derived Antioxidants: A Single-Blind Case-Control Clinical Study. Oxid Med Cell Longev. 2016;2016:4389410. doi: 10.1155/2016/4389410

Glynis A. A Double-blind, Placebo-controlled Study Evaluating the Efficacy of an Oral Supplement in Women with Self-perceived Thinning Hair. J Clin Aesthet Dermatol. 2012;5(11):2834. PMCID: PMC3509882

Proksch, E., Schunck, M., Zague, V., Segger, D., Degwert, J., & Oesser, S. (2014). Oral intake of specific bioactive collagen peptides reduces skin wrinkles and increases dermal matrix synthesis. Skin pharmacology and physiology, 27(3), 113119. DOI: 10.1159/000355523

Proksch, E., Segger, D., Degwert, J., Schunck, M., Zague, V., & Oesser, S. (2014). Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin pharmacology and physiology, 27(1), 4755. DOI: 10.1159/000351376

Kumar, S., Sugihara, F., Suzuki, K., Inoue, N., & Venkateswarathirukumara, S. (2015). A double-blind, placebo-controlled, randomised, clinical study on the effectiveness of collagen peptide on osteoarthritis. Journal of the science of food and agriculture, 95(4), 702707. DOI: 10.1002/jsfa.6752

Bello, A. E., & Oesser, S. (2006). Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: a review of the literature. Current medical research and opinion, 22(11), 22212232. DOI: 10.1185/030079906X148373

Hexsel, D., Zague, V., Schunck, M., Siega, C., Camozzato, F. O., & Oesser, S. (2017). Oral supplementation with specific bioactive collagen peptides improves nail growth and reduces symptoms of brittle nails. Journal of cosmetic dermatology, 16(4), 520526. DOI: 10.1111/jocd.12393

Glycine

Razak MA, Begum PS, Viswanath B, Rajagopal S. Multifarious Beneficial Effect of Nonessential Amino Acid, Glycine: A Review. Oxid Med Cell Longev. 2017;2017:1716701.  doi: 10.1155/2017/1716701

Wang, W., Wu, Z., Dai, Z., Yang, Y., Wang, J., & Wu, G. (2013). Glycine metabolism in animals and humans: implications for nutrition and health. Amino acids, 45(3), 463477. DOI: 10.1007/s00726-013-1493-1

Bannai M, Kawai N, Ono K, Nakahara K, Murakami N. The effects of glycine on subjective daytime performance in partially sleep-restricted healthy volunteers. Front Neurol. 2012;3:61. Published 2012 Apr 18. doi: 10.3389/fneur.2012.00061

De Paz-Lugo P, Lupiáñez JA, Meléndez-Hevia E. High glycine concentration increases collagen synthesis by articular chondrocytes in vitro: acute glycine deficiency could be an important cause of osteoarthritis. Amino Acids. 2018;50(10):1357-1365. doi: 10.1007/s00726-018-2611-x

Li, P., & Wu, G. (2018). Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth. Amino acids, 50(1), 2938. DOI: 10.1007/s00726-017-2490-6

Kasznel, A. J., Zhang, Y., Hai, Y., & Chenoweth, D. M. (2017). Structural Basis for Aza-Glycine Stabilization of Collagen. Journal of the American Chemical Society, 139(28), 94279430. DOI: 10.1021/jacs.7b03398

Clements, K. A., Acevedo-Jake, A. M., Walker, D. R., & Hartgerink, J. D. (2017). Glycine Substitutions in Collagen Heterotrimers Alter Triple Helical Assembly. Biomacromolecules, 18(2), 617624. DOI: 10.1021/acs.biomac.6b01808

Vieira, C. P., De Oliveira, L. P., Da Ré Guerra, F., Dos Santos De Almeida, M., Marcondes, M. C., & Pimentel, E. R. (2015). Glycine improves biochemical and biomechanical properties following inflammation of the achilles tendon. Anatomical record (Hoboken, N.J. : 2007), 298(3), 538545. DOI: 10.1002/ar.23041

Vieira, C. P., Viola, M., Carneiro, G. D., D'Angelo, M. L., Vicente, C. P., Passi, A., & Pimentel, E. R. (2018). Glycine improves the remodeling process of tenocytes in vitro. Cell biology international, 42(7), 804814. DOI: 10.1002/cbin.10937

Vieira, C. P., De Oliveira, L. P., Da Ré Guerra, F., Marcondes, M. C., & Pimentel, E. R. (2016). Green Tea and Glycine Modulate the Activity of Metalloproteinases and Collagen in the Tendinitis of the Myotendinous Junction of the Achilles Tendon. Anatomical record (Hoboken, N.J. : 2007), 299(7), 918928. DOI: 10.1002/ar.23361

Proline

Vance L Albaugh, Kaushik Mukherjee, Adrian Barbul, Proline Precursors and Collagen Synthesis: Biochemical Challenges of Nutrient Supplementation and Wound Healing, The Journal of Nutrition, Volume 147, Issue 11, November 2017, Pages 20112017. DOI: 10.3945/jn.117.256404

 Barbul A. (2008). Proline precursors to sustain Mammalian collagen synthesis. The Journal of nutrition, 138(10), 2021S2024S. DOI: 10.1093/jn/138.10.2021S

Wu, G., Bazer, F. W., Burghardt, R. C., Johnson, G. A., Kim, S. W., Knabe, D. A., Li, P., Li, X., McKnight, J. R., Satterfield, M. C., & Spencer, T. E. (2011). Proline and hydroxyproline metabolism: implications for animal and human nutrition. Amino acids, 40(4), 10531063. DOI: 10.1007/s00726-010-0715-z

Hydroxyproline

Shigemura Y, Iwasaki Y, Tateno M, et al. A Pilot Study for the Detection of Cyclic Prolyl-Hydroxyproline (Pro-Hyp) in Human Blood after Ingestion of Collagen Hydrolysate. Nutrients. 2018;10(10):1356. Published 2018 Sep 22. doi: 10.3390/nu10101356

Qiu, B., Wei, F., Sun, X., Wang, X., Duan, B., Shi, C., Zhang, J., Zhang, J., Qiu, W., & Mu, W. (2014). Measurement of hydroxyproline in collagen with three different methods. Molecular medicine reports, 10(2), 11571163. DOI: 10.3892/mmr.2014.2267

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