Y04801 Recombinant Human Vitronectin

Characteristics:

Source

Chinese Hamster Ovary cell line

Description

Human Vitronectin (Asp20-Leu478)

Accession #P04004

Predicted molecular mass

52.3kDa

Specification:

Appearance

White powder, Colorless clear liquid after reconstitution

Purity

≥95%, by SDS-PAGE (under reducing (R) & Non-reducing conditions, visualized by Coomassie staining)

Endotoxin

≤1 EU/mg by the LAL method

Activity

Measured by the ability of the immobilized protein to support the adhesion of B16-F1 mouse melanoma cells. The ED₅₀ for this effect is 2-10 μg/mL.

Optimal concentration depends on cell type as well as the application or research objectives.

Formulation

Lyophilized from a 0.22 μm-filtered solution containing PBS, 5% mannitol and 0.01% Tween 80, pH 7.4

Size

50 μg/vial, 1 mg/vial

Handling and Storage:

Reconstitution

It is recommended to redissolve in sterile deionized water.

Shipping

The product is shipped with blue ice.

Storage & Stability

24 months at -20°C to -80°C in lyophilized state

7-10 days at 2°C to 8°C under sterile conditions after reconstitution

6 months at -20°C to -80°C under sterile conditions after reconstitution

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

Background:

The protein 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. [provided by RefSeq, Aug 2020].

Vitronectin (VN) is an abundant adhesive glycoprotein in blood plasma and is found associated with different extracellular matrix sites, the vessel wall, and tumor cells, particularly upon tissue remodeling, injury/repair, or under disease conditions. Plasma VN is a structurally labile molecule that may be converted into a multimeric/multivalent form by interaction with various (hemostatic) factors or through surface binding. Mature VN is composed of several functionally unique binding domains for different interaction partners along the protein sequence that are mainly concentrated within the amino- and carboxy-terminal parts of the protein. Starting at the amino-terminus, these are the ‘‘somatomedin-B’’ (SMB) domain, the Arg-Gly-Asp (RGD) adhesion motif followed by an adjacent acidic epitope (due to sulfation and phosphorylation sites) that is part of the binding site for high molecular weight kininogen (HK), a long connecting segment encompassing a collagen binding domain, followed by two substructured hemopexin-like domains within the carboxy-terminal portion of the protein. These distinct binding domains endow VN acts as a potent matricellular factor, coordinating cell migration with pericellular proteolysis and growth factor signaling at sites of tissue remodeling or in tumors. The glycosylated form of human VN (459 amino acid residues) has a molecular mass of 75 to 78 kDa and circulates as single-chain (65 kDa) and/or disulfide-bridged twochain (10 to 12 kDa) forms, the latter being genetically determined by the amino acid residue at position 381 and derived from proteolytic cleavage in the carboxy-terminal region. A Met381Thr polymorphism increases the risk by 18-fold of hemangioblastoma in patients with von-Hippel-Lindau gene defect, possibly related to enhanced tumor angiogenesis.