Collagen solution from bovine skin

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Collagen solution from bovine skin
Product Infomation
Cat.No. NAT-0008
Product Name Collagen solution from bovine skin
Synonyms Collagen
Morphology & Appearance sterile-filtered Liquid
Surface coverage 6-10 μg/cm2
Components Type I Collagen differs from other Collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two α1 chains and one α2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.
impurities endotoxin ≤1.0 μmol/mg protein
Source bovine skin
Storage 2-8°C
Concentration 6 mg/mL
Application This highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D Collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals
Usage This product is prepared from type I bovine Collagen purified and extracted from tendon and skin and contains a high monomer content. The raw Collagen used to prepare this product has been isolated from a closed herd and purified with a GMP manufacturing process that includes inactivation of any possible prion or viral contamination. As supplied, it is a 3 mg/mL aqueous solution in 0.01 M HCl with a pH of 2.0. Collagen denatures when exposed to high temperatures or irradiation. Prior to a pH adjustment, store stock or diluted solutions refrigerated. Follwing a pH adjustment to 7, solutions should not exceed 40°C and should not be frozen.
Warning This product ships on wet ice and with recommended storage at 2-8°C, the product will last for 2 years.
Description Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. In 3D environments, cell extensions can use integrins on cell surfaces to activate specific signaling pathways and integran-independent mechanical interactions resulting from the entanglement of matrix fibrils is possible.
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