Background:

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.|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.|Belongs to the type IV collagen family.|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.|

Classification:

Primary antibody

Alternative names:

Collagen IV α2 ;Cleaved-Ser1485; Collagen alpha-2;IV chain [Cleaved into: Canstatin;

Species reactivity:

Human, Mouse

Host:

Rabbit

Isotype:

IgG

Immunogen:

Synthesized peptide derived from human Collagen IV α2 (Cleaved-Ser1485)

Concentration:

1 mg/ml

Molecular weight:

188320

Applications:

WB, ELISA

Storage:

-20°C for 1 year

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