BUGA-CoL Succinated Type I Atelocollagen in Water Soluble, BSE Free
Product Information
BUGA-CoL Succinated Type I Atelocollagen in Water Soluble, BSE Free is a product manufactured to medical-grade purity, setting the standard for all collagens in terms of purity (>99.9% collagen content), functionality, and natural collagen properties.
BUGA-Atelocol-SC undergoes FDA-approved viral inactivation studies. The raw materials are sourced from countries free from TSE/BSE, and production is carried out in compliance with TSE EN ISO 22442 1-2-3 standards. The certificate of analysis confirming the absence of TSE/BSE residues is provided using European Pharmacopoeia (EP 2.6.14 Method C) and United States Pharmacopoeia (USP <85>) test methods.
BUGA-Atelocol-SC is a water-soluble atelocollagen composed of approximately 97% Type I collagen, with the remainder being Type III collagen. This product is supplied in lyophilized powder form.
• Weigh the required amount of succinated collagen product in lyophilized fibrous/powder form according to your working protocol and transfer it into a mixing container.
• Add 0.01 N hydrochloric acid or 0.5 M acetic acid solution according to the concentration you will work with and mix.
• Since it can also dissolve in pure water, physiological serum, or neutral environments, you can use these solvents depending on the concentration you are working with.
• If the prepared solution is not to be used immediately, it can be stored in the refrigerator at +4 °C. Do not freeze and thaw the solution.
Succinated collagen (SC) is soluble at physiological pH and is therefore an ideal candidate for injectable biomaterials. The film obtained from **BUGA-Atelocol-SC** provides the necessary transparency for ophthalmic applications.
• Prosthetic Coatings
• Implant Materials
• Tissue Engineering
• Biomaterials
• Tissue Scaffolds
• Foams
• Sponges
• Suspensions
• Coatings
• Pastes
• Films
• Sheets
Technical Specifications of the Product
Appearance | Lyophilized Fibrous Powder | |
Smell | No Data Available | |
Extraction Method | Enzymatic Succinylated Atelocollagen | |
Sterilization Method | Filtration | |
Solubility/Collagen Concentration | 1, 3, 6 mg/ml (in purified water) | |
Storage Temperature | +4 ºC | |
Shelf Life | 2 years from the date of manufacture | |
Collagen Purity - Silver Staining | ~98,9 | |
Source (Animal Species) | Bovine Tendon | |
Degree of Succinylation | ≥%80 | |
Endotoxin/LAL European Pharmacopoeia (EP 2.6.14 Method C) United States Pharmacopoeia (USP <85>) | <0,5 EU/ml | |
Microbiological Analysis United States Pharmacopoeia (USP <61>) | Aerobic Mesophilic Bacterial CFU/ml | <10 |
Anaerobic Mesophilic Bacteria (30°C) CFU/ml | <10 | |
Fungi-Yeast CFU/ml | <10 | |
• 조한희. (2004). A study of calcification-inducing succinylated type I atelocollagen (Doctoral dissertation, Graduate School, Yonsei University).
• 류동진. (2010). The effects of succinylated atelocollagen and adenosine on periorbital wrinkles (Doctoral dissertation, 연세대학교 대학원).
• Tsujigiwa, H., Nagatsuka, H., Gunduz, M., Rodriguez, A., Rivera, R. S., LeGeros, R. Z., ... & Nagai, N. (2005). Effects of immobilized recombinant human bone morphogenetic protein‐2/succinylated type I atelocollagen on cellular activity of ST2 cells. Journal of Biomedical Materials Research Part A: An Official Journal of The Society for Biomaterials, The Japanese Society for Biomaterials, and The Australian Society for Biomaterials and the Korean Society for Biomaterials, 75(1), 210-215.
• Shin, J. U., Roh, M. R., Rah, D. K., Ae, N. K., Suh, H., & Chung, K. Y. (2011). The effect of succinylated atelocollagen and ablative fractional resurfacing laser on striae distensae. Journal of Dermatological Treatment, 22(2), 113-121.
• Ryu, D. J., Jung, J. Y., Chung, K. Y., Suh, H., Oh, S. H., & Lee, J. H. (2013). The Efficacy and Safety of Succinylated Atelocollagen and Adenosine for the Treatment of Periorbital Wrinkles.
• Zhang, J., Sui, P., Yang, W., Shirshin, E. A., Zheng, M., Wei, B., ... & Wang, H. (2023). Site-specific modification of N-terminal α-amino groups of succinylated collagen. International Journal of Biological Macromolecules, 225, 310-317.
• Tsujigiwa, H., Rodriguez, A. P., Takagi, T., Long, H. H., Rui, K., Lu, Z., ... & Xiao, J. (2006). Effects of Immobilized rhBMP-2/atelocollagen in vivo and in vitro. Journal of Hard Tissue Biology, 15(1), 27-33.
• Yamachika, E., Tsujigiwa, H., Shirasu, N., Ueno, T., Sakata, Y., Fukunaga, J., ... & Sugahara, T. (2009). Immobilized recombinant human bone morphogenetic protein‐2 enhances the phosphorylation of receptor‐activated Smads. Journal of Biomedical Materials Research Part A: An Official Journal of The Society for Biomaterials, The Japanese Society for Biomaterials, and The Australian Society for Biomaterials and the Korean Society for Biomaterials, 88(3), 599-607.
• Zhang, J., Sui, P., Yang, W., Shirshin, E. A., Zheng, M., Wei, B., ... & Wang, H. (2023). Site-specific modification of N-terminal α-amino groups of succinylated collagen. International Journal of Biological Macromolecules, 225, 310-317.
