Collagen alpha-1(I) chain (UniProt P02452; also known as Alpha-1 type I collagen) is encoded by the COL1A1 gene (Gene ID 1277) in human. Collagen is the major component of the extracellular matrix (ECM) and form the fibrils of tendons, ligaments, and bones. Type I collagen consists of two alpha I chains and one alpha 2 chain. Alpha-1 type I collagen is initially produced as an 1464-amino acid prepro-form with a signal peptide sequence (a.a. 1-22) and two propeptide sequences (a.a. 23-161 and a.a. 1219 -1464), the removal of which yields the mature alpha-1(I) chain. The mature alpha-1(I) chain is composed mostly of a large triple-helical region (a.a. 179-1192) sandwiched between two nonhelical segments known as the N-terminal telopeptide (a.a. 162-178; numbering based on the prepro-form) and the C-terminal telopeptide (a.a. 1193-1218; numbering based on the prepro-form). Collagen can be extracted from tissue via either enzymatic or non-enzymatic means. Collagen extracted using the proteolytic enzyme pepsin corresponds to the large triple-helical region, referred to as atelocollagen because both the N- and C-terminal telopeptides have been cleaved off by pepsin. On the other hand, collagen preparations obtained with non-enzymatic means (e.g. by acid extraction) have the intact telopeptides at both ends.
Synonyms: Pro-collagen alpha-1(I) chain, Pro-Alpha-1 type I collagen
Application: Western Blotting Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung and skin tissue lysate.Flow Cytometry Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung tissue.Immunohistochemistry Analysis: A representative lot detected Pro-Collagen Type I, A1/COL1A1 in mouse lung tissue.
Other Notes: Concentration: Please refer to lot specific datasheet.