Simple Plex Discovery Human Pro-Collagen I alpha 1 New

Simple Plex Discovery Human Pro-Collagen I alpha 1 Summary

*The Sample Volume represented is based on the amount of sample incorporated into the reaction after taking into account the assay’s minimum required dilution for a given matrix. Serial dilution may be necessary to achieve some of the final sample volumes represented.

Product Summary

Precision

Cell Culture Supernates, Serum, EDTA Plasma, Heparin Plasma

Recovery

Linearity

Product Datasheets

Preparation and Storage

Background: Pro-Collagen I alpha 1

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 300 nm 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 alpha 1(I) chains and one alpha 2(I) chain, although homotrimers consisting of three identical alpha 1(I) chains have also been described. This recombinant mini pro-alpha 1(I) collagen consists of a shortened alpha 1(I) chain 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 (alpha 1) and the C-terminal propeptide. This truncated pro-alpha 1(I) collagen is a substrate for procollagen N-proteinase and procollagen C-proteinase.

Related Research Areas

• Extracellular Matrix Molecules
• Molecules Secreted by VSMC
• Osteogenesis Markers
• Osteoprogenitor Markers