Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a procollagen molecule which is characterized by a 300nm triple helical domain flanked by globular N- and C-terminal propeptides. The triple helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues. Type I collagen is a heterotrimer that consists of two alpha1(I) chains and one alpha2(I) chain, although homotrimers consisting of three identical alpha1 (I) chains have also been described. This recombinant mini pro-alpha1(I) collagen is a homotrimer of three shortened alpha1(I) chains with following domain structure from N-to C-terminus: N-propeptide, N-telopeptide, the 33 most N-terminal Gly-Xaa-Yaa repeats, the 33 most C-terminal Gly-Xaa-Yaa repeats, C-telopeptide and C-propeptide. The preparation contains a mixture of the full-length molecule, pN collagen I(alpha1) and the C-terminal propeptide. This truncated pro-alpha1(I) collagen is a substrate for procollagen N-proteinase and procollagen C-proteinase.
Source:
Chinese Hamster Ovary cell line, CHO-derived Gln23-Lys277+Gly1094-Leu1464, with an N-terminal human CD33 signal sequence and 6-His tag.
SDS-PAGE:
79-83kD, 54-56kD, 35-36kD, reducing conditions
Activity:
Measured by the cleavage of its C-terminal propeptide by recombinant human BMP-1. 50% of full-length Pro Collagen I alpha1 is cleaved by rhBMP-1.
Endotoxin Level: (same/less than)1EU/1ug (LAL)
Storage and Stability:
Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
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