Mouse anti-Human COL4A1 Monoclonal Antibody

Uniprot Id

P02462

Target Species

Human

Target Name

COL4A1

Target Full Name

Collagen alpha-1(IV) chain

Target 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.; Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation.

Target Involvement

Brain small vessel disease with or without ocular anomalies (BSVD); Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC); Porencephaly 1 (POREN1); Intracerebral hemorrhage (ICH); Tortuosity of retinal arteries (RATOR); Schizencephaly (SCHZC)

Target Subcellular Location

Secreted, extracellular space, extracellular matrix, basement membrane.

Target Protein Families

Type IV collagen family

Target Tissue Specificity

Highly expressed in placenta.

Target Research Area

Cancer

Target Synonyms

Arresten; BSVD; CO4A1_HUMAN; COL4A1; COL4A1 NC1 domain; COL4A2; COL4A3; COL4A4; COL4A5; collagen alpha-1(IV) chain; Collagen IV Alpha 1 Polypeptide; Collagen IV Alpha 2 Polypeptide; Collagen Of Basement Membrane Alpha 1 Chain; Collagen Of Basement Membrane Alpha 2 Chain; Collagen Type IV Alpha 1; collagen type IV alpha 1 chain; Collagen Type IV Alpha 2; Collagen Type IV Alpha 3; Collagen Type IV Alpha 4; Collagen Type IV Alpha 5; RATOR

Target Background

This gene encodes a type IV collagen alpha protein. Type IV collagen proteins are integral components of basement membranes. This gene shares a bidirectional promoter with a paralogous gene on the opposite strand. The protein consists of an amino-terminal 7S domain, a triple-helix forming collagenous domain, and a carboxy-terminal non-collagenous domain. It functions as part of a heterotrimer and interacts with other extracellular matrix components such as perlecans, proteoglycans, and laminins. In addition, proteolytic cleavage of the non-collagenous carboxy-terminal domain results in a biologically active fragment known as arresten, which has anti-angiogenic and tumor suppressor properties. Mutations in this gene cause porencephaly, cerebrovascular disease, and renal and muscular defects. Alternative splicing results in multiple transcript variants.