Human Vitronectin N-GST (cell-binding domain)
This recombinant VN fragment corresponds to the cell-binding domain. It is expressed as a GST-tagged fusion protein in E. coli, liberated from inclusion bodies by urea treatment, and purified over heparin–agarose.
Vitronectin (VN) is a 75-kDa adhesive glycoprotein that also plays a role in regulating several proteolytic enzyme cascades including complement, thrombosis, and fibrinolysis. Several distinct, biologically active conformations of VN are known to exist. In the blood, VN circulates in a monomeric form. High molecular mass oligomers of VN are found within the extracellular matrix (ECM)1 and in platelet releasate. The interaction of vitronectin with thrombin–antithrombin III complexes, plasminogen activator inhibitor, or with chemical or thermal denaturants results in conformational changes that lead to VN multimerization. These conformational changes may be important for VN activity as the multimeric form of VN preferentially binds to v 3 and IIb 3 integrins, urokinase receptors, plasminogen activator inhibitor, and glycosaminoglycans. The interaction of multimeric VN with these ligands affects a number of functions including cell adhesion and spreading, cell migration, inflammation, and hemostasis.
From the laboratory of Denise C. Hocking, PhD, University of Rochester Medical Center.
Part of The Investigator's Annexe program.
This recombinant VN fragment corresponds to the cell-binding domain. It is expressed as a GST-tagged fusion protein in E. coli, liberated from inclusion bodies by urea treatment, and purified over heparin–agarose.
Vitronectin (VN) is a 75-kDa adhesive glycoprotein that also plays a role in regulating several proteolytic enzyme cascades including complement, thrombosis, and fibrinolysis. Several distinct, biologically active conformations of VN are known to exist. In the blood, VN circulates in a monomeric form. High molecular mass oligomers of VN are found within the extracellular matrix (ECM)1 and in platelet releasate. The interaction of vitronectin with thrombin–antithrombin III complexes, plasminogen activator inhibitor, or with chemical or thermal denaturants results in conformational changes that lead to VN multimerization. These conformational changes may be important for VN activity as the multimeric form of VN preferentially binds to v 3 and IIb 3 integrins, urokinase receptors, plasminogen activator inhibitor, and glycosaminoglycans. The interaction of multimeric VN with these ligands affects a number of functions including cell adhesion and spreading, cell migration, inflammation, and hemostasis.
From the laboratory of Denise C. Hocking, PhD, University of Rochester Medical Center.
Part of The Investigator's Annexe program.
| Product Type: | Protein |
| Name: | Recombinant Human Vitronectin (cell binding domain); amino acids 42-126. |
| Accession ID: | P04004 |
| Source: | Human protein expressed in E. coli DH5 alpha carrying the cloned gene in pGEX-2T |
| Molecular Weight: | 35581.5 Da |
| Amino Acid Sequence: | >QVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPG |
| Fusion Tag(s): | GST, N-terminal |
| Purity: | > 90% by SDS-PAGE |
| Buffer: | Solution in PBS |
| Concentration: | 3.9mg/mL |
| Storage: | Store at -80C |
| Shipped: | Dry ice |
Cell binding domain.
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