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Human Collagen Type IV



1 mg
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Specificity: Collagen Type IV, Human

Preservative: None Type of Product: Purified Collagens

Inactivation: Pepsin digestion and storage in 500mM Acetic acid.

Buffer: 500mM Acetic acid

Applications Notes : Type IV collagen standard. Antigen for antibody production. Coating material for cell culture studies. Formation of collagen gels. Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded. Concentration: Concentration is lot specific Human Collagen Type IV

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 endothelial cell proliferation and angiogenesis. Inhibits angiogenesis potentially via mechanisms involving cell surface proteoglycans and the alpha and beta integrins of endothelial cells.

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.

Subcellular Location: Secreted, extracellular space, extracellular matrix, basement membrane.

Tissue Specificity: Highly expressed in placenta.

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.

Ptm: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.

Ptm: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

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.

Ptm: The trimeric structure of the NC1 domains may be stabilized by covalent bonds between Lys and Met residues.

Disease: Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage [MIM:607595]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.

Disease: Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy, aneurysms, and muscle cramps (HANAC) [MIM:611773]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.

Disease: Defects in COL4A1 are a cause of porencephaly type 1 [MIM:175780]; also known as encephaloclastic porencephaly. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Inheritance is autosomal dominant.

Similarity: Belongs to the type IV collagen family.

Similarity: Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.

Additional Information

Name Human Collagen Type IV
Related Product Names Human Collagen Type IV; Arresten Human Collagen Type IVCOL4A1
NCBI Acc Number NP_001836.2
Molecular Weight 160615
Datasheets / Downloads GWB-14E8D9 Datasheet
Swiss Prot Number P02462
Purity >90% pure (SDS-PAGE) Controlled and limited pepsin digestion, followed by selective salt precipitation
Source Placental villi
Applications ELISA
Format Purified, Liquid
Storage The collagen may be transferred into physiological buffers by dialysis at 2-8 C. Purified collagen may be stored for several months at 2-8 C without appreciable loss of activity. For long term storage, aliquot and store at -20 C. Avoid multiple freeze/tha
Intended Use Research Use Only