Rabbit anti-Human Vitronectin Polyclonal Antibody

Uniprot Id

P04004

Target Species

Human

Target Name

VTN

Target Full Name

Vitronectin

Target Function

Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

Target Subcellular Location

Secreted, extracellular space.; Parasitophorous vacuole.

Target Tissue Specificity

Expressed in the retina pigment epithelium (at protein level). Expressed in plasma (at protein level). Expressed in serum (at protein level).

Target Research Area

Cardiovascular

Target Synonyms

Complement S Protein; Epibolin; S Protein; S-protein; Serum Spreading Factor; Serum-spreading factor; Somatomedin B; Somatomedin-B; V75; Vitronectin; Vitronectin V10 subunit; Vitronectin V65 subunit; VN; VNT; VTN; VTNC_HUMAN

Target Background

The protein encoded by this gene functions in part as an adhesive glycoprotein. Differential expression of this protein can promote either cell adhesion or migration as it links cells to the extracellular matrix through a variety of ligands. These ligands include integrins, plasminogen activator inhibitor-1, and urokinase plasminogen activator receptor. This secreted protein can be present in the plasma as a monomer or dimer and forms a multimer in the extracellular matrix of several tissues. This protein also inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to several serpin serine protease inhibitors. This protein can also promote extracellular matrix degradation and thus plays a role in tumorigenesis. It is involved in a variety of other biological processes such as the regulation of the coagulation pathway, wound healing, and tissue remodeling. The heparin-binding domain of this protein give it anti-microbial properties. It is also a lipid binding protein that forms a principal component of high density lipoprotein.