Vitronectin [VIT-2]

GWB-4FE67B

IgM

Human

Vitronectin

0. 1% Sodium Azide

Extracellular Vitronectin (also known as serum-spreading factor S-protein of complement or epibolin) is one of the major multifunctional cell-adhesive glycoproteins in mammalian plasma and serum. It is a monomeric acidic glyco-protein detected as a mixture of 75 kD and 65 kD polypeptides. Vitronectin binds to heparin collagen streptococci and variety of cultured cells. It also acts as an inhibitor of the complement cascade by binding to the C5b-9 complex. Vitronectin promotes cell adhesion and spreading by binding through its cell-attachment tripeptide Arg-Gly-Asp (RG-D) activity which is mediated by several different integrin receptors. Apart from the significance for identifying the molecule in the above situations it also plays an important role in events such as embryonal development deposition of vitronectin in a number of fibrotic disease states carcinomas and metastases.

Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

Secreted extracellular space.

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.

N- and O-glycosylated (By similarity).

It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Contains 1 SMB (somatomedin-B) domain.