VTN
VTN (vitronectin, also known as VN, serum spreading factor, somatomedin B or complement S-protein) is a secreted adhesive glycoprotein that links cells to the extracellular matrix. It also regulates complement, coagulation and tissue remodelling. Browse Assay Genie's current range of VTN research reagents below, or read on for the biology behind the target.
VTN functions in part as an adhesive glycoprotein. Differential expression of this protein can promote either cell adhesion or migration, because it links cells to the extracellular matrix through a range of ligands. These include integrins, plasminogen activator inhibitor-1 and the urokinase plasminogen activator receptor. The protein also binds several serpin serine protease inhibitors, and it inhibits the membrane-damaging effect of the terminal cytolytic complement pathway.
The VTN protein is secreted. It can be present in plasma as a monomer or dimer, and it forms a multimer in the extracellular matrix of several tissues. Its heparin-binding domain gives it anti-microbial properties. It is also a lipid-binding protein and a principal component of high density lipoprotein. UniProt records the somatomedin-B region as a growth hormone-dependent serum factor with protease-inhibiting activity, and lists the parasitophorous vacuole as a further location alongside the extracellular space. The mouse ortholog is Vtn.
VTN is involved in the regulation of the coagulation pathway, wound healing and tissue remodelling. It can also promote extracellular matrix degradation, and so plays a role in tumorigenesis. HGNC classes the VTN gene among receptor ligands and complement system regulators and receptors. Its earlier names, serum spreading factor, somatomedin B and complement S-protein, reflect the range of activities described for this protein.
VTN links cells to the extracellular matrix through integrins and the urokinase plasminogen activator receptor, so it is a useful ligand for studying adhesion and migration.
VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, which makes it relevant to complement regulation research.
VTN binds serpins such as plasminogen activator inhibitor-1 and takes part in coagulation, wound healing and tissue remodelling.
VTN can promote extracellular matrix degradation and is linked to tumorigenesis, so researchers study it in cancer biology and matrix remodelling.
VTN is a secreted adhesive glycoprotein that links cells to the extracellular matrix through integrins, plasminogen activator inhibitor-1 and the urokinase plasminogen activator receptor. It inhibits the terminal complement pathway, binds serpins, and contributes to coagulation, wound healing and tissue remodelling.
The gene symbol is VTN, with VN as an alias. Earlier names for vitronectin include serum spreading factor, somatomedin B and complement S-protein. These names reflect its roles in cell spreading, growth hormone-dependent serum activity and complement regulation.
NCBI Gene notes that VTN can promote extracellular matrix degradation and so plays a role in tumorigenesis. The mouse ortholog is Vtn. For reactivity with a given species, check the datasheet of any product for its validated reactivity.
Integrins, serpins, urokinase receptor and other adhesion and complement-related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04004; product specifications from Assay Genie datasheets.