BUGA-CoL Type I Atelocollagen from Bovine Tendon, Lyophilized, BSE-Free

Product Information
BUGA-CoL Type I Atelocollagen from Bovine Tendon Lyophilized, BSE-Free (BUGA-AteloCol) is a medical-grade product that sets the standard for all collagens in terms of purity (>99.9% collagen content), functionality, and natural collagen properties. BUGA-AteloCol is subjected to FDA-approved viral inactivation studies. It is produced in compliance with TSE EN ISO 22442 1-2-3 standards using raw materials sourced from countries with a non-TSE/BSE status. The absence of TSE/BSE residues is confirmed with an analysis certificate using European Pharmacopoeia (EP 2.6.14 Method C) and United States Pharmacopoeia (USP <85>) testing methods.
BUGA-AteloCol is a soluble atelocollagen composed of approximately 97% Type I collagen and the remainder as Type III collagen. This product is available in a lyophilized powder form containing 15 mg of bovine collagen. When dissolved in 5 ml of sterile 0.01 N HCl, it yields a concentration of approximately 3 mg/ml.
BUGA-AteloCol can be coated onto tissue culture plates as a substrate for culturing primary cells such as keratinocytes and hepatocytes. It can also be prepared as a gel to provide a 3D matrix or surface coating designed for healing wounds, burns, or damaged tissues. BUGA-AteloCol collagen is recommended for surface coatings and cell culture studies through the preparation of thin layers. The BUGA-AteloCol collagen product is offered in user-friendly packaging and supplied as a sterile lyophilized powder for convenient storage.
• 3D Collagen Sponges (Cell Culture)
• Protein Delivery and Drug Release Systems
• Nanofiber Drug Delivery Systems
• Sealing (Bandage) Products
• Medical Device Coatings
• Hemostats
• Bioinks
• Biomaterials
• Tissue Scaffolds
• Sponges
o Weigh the appropriate amount of BUGA-AteloCol product as needed for your work and/or determine its concentration, then transfer it to a suitable volume container.
o After weighing the lyophilized product, prepare a 0.01 M hydrochloric acid or 0.5 M acetic acid solution according to the working volume.
o Dissolve the lyophilized product in the prepared acid solution in a suitable mixing container (e.g., borosilicate beaker or bottle) with a magnetic stir bar and stirrer at a slow rpm speed (preferably 350-500 rpm) until fully dissolved. You can also dissolve it by pipetting.
o If you are not going to use the prepared solution immediately, store it at 2-8 °C.
o Note: Freezing the dissolved product is not recommended.
o Important Note: Do not apply rapid stirring, shaking, or vortexing after preparing the solution, as it may cause cross-linking in the product.
o For cell culture studies, you can apply the following protocol:
o Prepare the BUGA-AteloCol product as described above.
o After preparing the solution, dilute it to the desired concentration with hydrochloric acid or acetic acid.
o After adding the solution to all wells, incubate at 37°C for 1 hour (the time may vary depending on solidification. Collagen maintains its soluble form at +4°C but solidifies at 37°C).
o Carefully remove the remaining solution or aspirate it with a pipette. Wash with PBS or serum-free medium to remove residual acid.
o The well plate can be used immediately or stored under sterile conditions at 2-8°C for up to 1 week.
Technical Specifications of the Product
Appearance | Lyophilized White Color | |
Smell | No Data Available | |
Extraction Method | Enzymatic - Atelocollagen | |
Sterilization Method | Filtration | |
Solubility/Collagen Concentration | 1, 3, 6 mg/ml (in 0.01 M HCl) | |
Storage Temperature | Store at -20 ºC. After preparation as a solution, store at 2-8 ºC. | |
Shelf Life | 2 years from the production date | |
Solution Shelf Life | 3 months after preparation as a solution (at +4 ºC) | |
Collagen Purity - Silver Staining | ~98,9 | |
Source (Animal Species) | Bovine Tendon | |
Endotoxin/LAL European Pharmacopoeia (EP 2.6.14 Method C) United States Pharmacopoeia (USP <85>) | <0,2 EU/ml | |
Microbiological Analysis United States Pharmacopoeia (USP <61>) | Aerobic Mesophilic Bacteria cfu/ml | <10 |
Anaerobic Mesophilic Bacteria (30 ℃) cfu/ml | <10 | |
Mold-Yeast cfu/ml | <10 | |
SDS PAGE (Molecular Weight and Impurity Determination) | α-1 and α-2 chains with a molecular weight of 125-150 kDa, and β and γ chains above 275 kDa are observed. |
Material Origin Certificate
Supplier | BUGAMED Biotechnology Industry and Trade Inc. |
Supplier Reference Number | BGM280817-2 |
Supplier Location | Eskişehir, TÜRKİYE |
Product Name/Class | BUGA-CoL Type I Atelocollagen from Bovine Tendon Lyophilized, BSE Free |
Animal Origin |
|
Animal Species | Cattle |
Tissue Origin | Tendon |
Country of Origin | Türkiye |
Non-Animal Origin Source |
|
Country of Origin | - |
Animal-Origin Risk Reduction Steps
| ISO 22442-1:2020 Medical devices utilizing animal tissues and their derivatives Part 1: Application of risk management ISO 22442-2:2020 Medical devices utilizing animal tissues and their derivatives Part 2: Controls on sourcing, collection and handling ISO 22442-3:2007 Medical devices utilizing animal tissues and their derivatives Part 3: Validation of the elimination and/or inactivation of viruses and transmissible spongiform encephalopathy (TSE) agents |
Production Method | Enzymatic Extraction |
Short Description of the Production Method
| Collagen is purified from bovine tendon through a multi-step process that includes chemical treatment, enzymatic extraction, viral inactivation, filtration, dialysis, pH control, lyophilization, and packaging steps. Production is conducted under the scope of ISO 22442, ISO 13485, and ISO 22716 Standards. |
• Sano, A., Maeda, M., Nagahara, S., Ochiya, T., Honma, K., Itoh, H., ... & Fujioka, K. (2003). Atelocollagen for protein and gene delivery. Advanced drug delivery reviews, 55(12), 1651-1677.
• Sorensen, J. R., Kaluhiokalani, J. P., Hafen, P. S., Deyhle, M. R., Parcell, A. C., & Hyldahl, R. D. (2019). An altered response in macrophage phenotype following damage in aged human skeletal muscle: implications for skeletal muscle repair. The FASEB Journal, 33(9), 10353-10368.
• Schwerdtfeger, L. A., Nealon, N. J., Ryan, E. P., & Tobet, S. A. (2019). Human colon function ex vivo: Dependence on oxygen and sensitivity to antibiotic. PLoS One, 14(5), e0217170.
• Cardoso, A. M., Sousa, M., Morais, C. M., Oancea-Castillo, L. R., Régnier-Vigouroux, A., Rebelo, O., ... & Jurado, A. S. (2019). MiR-144 overexpression as a promising therapeutic strategy to overcome glioblastoma cell invasiveness and resistance to chemotherapy. Human molecular genetics, 28(16), 2738-2751.
• Raouf, E. I., Kobayashi, M. F., AbdEl-Aal, A. B. M., Zhang, Y., & Miron, R. J. (2017). Novel bioabsorbable bovine derived atelo-collagen type I membrane: Characterization into host tissues. Periodon Prosthodon, 3, 1.
• Suh, D. S., Lee, J. K., Yoo, J. C., Woo, S. H., Kim, G. R., Kim, J. W., ... & Song, H. S. (2017). Atelocollagen enhances the healing of rotator cuff tendon in rabbit model. The American journal of sports medicine, 45(9), 2019-2027.
• López García, J. A., Humpolíček, P., Lehocký, M., Junkar, I., & Mozetič, M. (2013). Different source atelocollagen thin films: Preparation, process optimisation and its influence on the interaction with eukaryotic cells. Materiali in tehnologije.
• Camacho-Chacon, J. A., Cuenca-Espierrez, J., Roda-Rojo, V., Martin-Martinez, A., Calderon-Meza, J. M., Alvarez-Alegret, R., & Martin-Hernandez, C. (2022). Bioinductive collagen implants facilitate tendon regeneration in rotator cuff tears. Journal of Experimental Orthopaedics, 9(1), 1-7.
• Øya, E., Becher, R., Ekeren, L., Afanou, A. K., Øvrevik, J., & Holme, J. A. (2019). Pro-inflammatory responses in human bronchial epithelial cells induced by spores and hyphal fragments of common damp indoor molds. International journal of environmental research and public health, 16(6), 1085.
• McClellan, A., Evans, R., Sze, C., Kan, S., Paterson, Y., & Guest, D. (2019). A novel mechanism for the protection of embryonic stem cell derived tenocytes from inflammatory cytokine interleukin 1 beta. Scientific Reports, 9(1), 2755.