Human Collagen I alpha 1 Antibody Summary
Gln23-Lys277 + Gly1094-Leu1464
Accession # P02452
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Human Collagen I alpha 1 ELISA Standard Curve. Recombinant Human Collagen I alpha 1 protein was serially diluted 2-fold and captured by Mouse Anti-Human Collagen I alpha 1 Monoclonal Antibody (Catalog # MAB62201) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human Collagen I alpha 1 Monoclonal Antibody (Catalog # MAB62202) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: 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 (1). 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 (1). 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 (2). 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.
- Canty, E.G. et al. (2005) J. Cell Sci. 118:1341.
- Han, S. et al. (2008) J. Mol. Biol. 383:122.
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