Type IV collagen has been found to play a key role in angiogenesis, neurological diseases and metastasis. Collagen from human placenta has been used to assess the bioelectric effects of quinine on airway epithelial cells, to study the selective toxicity of engineered lentvirus lytic peptides and in a particle aggregation assay for the rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus. It has also been used in a magnesium-dependent, collagen-binding assay during characterization of human lung tumor-associated antigens.
During development, collagen IV is ubiquitously distributed in BMs. During the maturation process, this network gets partially replaced in a remarkably tissue specific manner, defining BM structure and function. Collagen IV has been shown to bind to platelets, hepatocytes, keratinocytes, endothelial, mesangial, pancreatic cells and some tumor cells.
Tissue injury in the autoimmune disease Goodpasture syndrome is due to pathogenic autoantibodies targeting the Collagen IV α3 chain . Mutations in COL4A5 are associated with Alport syndrome.
All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type IV collagen occurs only in the basement membranes and contains up to six genetically distinct a-chains.
This product should be stored desiccated at -20°C, and will retain activity in these conditions for 3 years.
This powder can be reconstituted in sterile .5 M acetic acid, PBS or water at 1 mg/mL. A PBS solution will be stable for at least one year at -20°C.
An SDS polyacrylamide gel electrophoresis test run under reducing conditions consistent with basement membrane collagen yields three major bands.
Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.