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Vitronectin

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Cat. No. Species Product Description Structure Purity Feature
VIN-H5119 Human Human Vitronectin / VTN Protein, Tag Free
VIN-H5119-structure
VIN-H5119-sds
VIN-H5119-elisa_1
VIN-H8113 Human Biotinylated Human Vitronectin / VTN Protein, Tag Free, ultra sensitivity (primary amine labeling)
VIN-H8113-structure
VIN-H8113-sds
VIN-H8113-elisa_1

Vitronectin Part of Bioactivity data

VIN-H8113-ELISA
Biotinylated Human Vitronectin, Tag Free, primary amine labelingBiotinylated Human Vitronectin, Tag Free, primary amine labeling (Cat. No. VIN-H8113) ELISA bioactivity

Immobilized Biotinylated Human Vitronectin, Tag Free, primary amine labeling (Cat. No. VIN-H8113) at 1 μg/mL (100 μL/well) on Streptavidin (Cat. No. STN-N5116) precoated (0.5 μg/well) plate, can bind Human ITGAV&ITGB5 Heterodimer Protein, His Tag&Tag Free (Cat. No. IT5-H52W5) with a linear range of 0.156-1.25 μg/mL (QC tested).

VIN-H5119-ELISA
Human Vitronectin, Tag FreeHuman Vitronectin, Tag Free (Cat. No. VIN-H5119) ELISA bioactivity

Immobilized Human Vitronectin, Tag Free (Cat. No. VIN-H5119) at 2 μg/mL (100 μL/well) can bind Human ITGAV&ITGB3 Heterodimer Protein, His Tag&Tag Free (Cat. No. IT3-H52E3) with a linear range of 0.078-1.25 μg/mL (QC tested).

Vitronectin Molecule Synonym Name

VTN,V75,VN,Vitronectin,S-protein,Serum-spreading factor

Vitronectin Molecule Background

Vitronectin is also known as S-protein, VN, VTN, V75. Vitronectin, a multifunctional glycoprotein, is involved in coagulation, inhibition of the formation of the membrane attack complex (MAC), cell adhesion and migration, wound healing, and tissue remodeling. The primary cellular source of vitronectin is hepatocytes. Blocking of Hic(a member of the pneumococcal surface protein C (PspC) family) by specific antiserum or genetic deletion significantly reduced pneumococcal binding to soluble and immobilised vitronectin and to Factor H, respectively. In addition, 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.

Vitronectin References

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