Collagen IV α2 (Cleaved-Ser1485) rabbit pAb

Domain: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain. function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. PTM: The trimeric structure of the NC1 domains may be stabilized by covalent bonds between Lys and Met residues. PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. similarity: Belongs to the type IV collagen family. similarity: Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain. subunit: There are six type IV collagen isoforms, alpha 1 (IV)-alpha 6 (IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.