ELK Biotechnology Collagen IV α2 (Cleaved-Ser1485) rabbit pAb

Collagen IV α2 (Cleaved-Ser1485) rabbit pAb

제품 정보

Background

Alpha chains of type IV collagen contain a non-collagenous domain (NC1) at the C-terminus and frequent interruptions of the G-X-Y repeats in the central triple-helical domain, which may confer flexibility. Type IV collagen is a major structural component of glomerular basement membranes (GBM), forming a “chicken-wire” meshwork with laminins, proteoglycans, and entactin/nidogen. It potently inhibits angiogenesis and tumor growth.

Post-translational Modifications (PTMs):

• Prolines at the third position of G-X-Y repeats are hydroxylated.
• NC1 domains may be stabilized by covalent bonds between Lys and Met residues.
• Contains multiple cysteine residues forming disulfide bonds, 12 of which are conserved in all type IV collagens.

Similarity and Structure:

• Belongs to the type IV collagen family.
• Contains one collagen IV NC1 (C-terminal non-collagenous) domain.
• Six isoforms (α1(IV)–α6(IV)) can form triple helices to generate the type IV collagen network.