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50μL&100μg $ 499.00
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For research use only.

Background
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.
Synonyms
N-Propeptide Of Type I Procollagen, P1NP, PINP, Procollagen I Amino Terminal Propeptide
Swissprot
Reactivity
Human
Specificity
Detects Human PⅠNP in ELISAs
Applications
ELISA
Storage
-20℃
Expiration date
12 months
Introduction
This Antibody Pair Kit applies to the sandwich ELISA assay.
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