VITRONECTIN

GWB-A2D7E2

The antibody can be used for immuno assays. Western blotting. immuno precipitation and purification. Furthermore the antibody is useful for flow cytometry. This monoclonal antibody binds to human vitronectin. It binds to soluble vitronectin as well as to membrane bound vitronectin. Monoclonal antibody BV1 recognizes human vitronectin. Vitronectin is an abundant glycoprotein (~75kDa) consisting of 459 amino acids. About one third of the protein molecular mass is composed of carbohydrates. Vitronectin is found in blood plasma and the extracellular matrix. Vitronectin is a multifunctional protein since it promotes attachment and spreading of animal cells in vitro it inhibits cytolysis by the complement C5b-9 complex and it modulates antithrombin III-thrombin action in blood coagulation. The protein consists of three domains: the N-terminal Somatomedin B domain (1-39) a central domain with hemopexin homology (131-342) and a C-terminal domain (347-459) also with hemopexin homology. The Somatomedin B domain binds to Plasminogen Activator Inhibitor-1 (PAI-1) and is responsible for PAI-1 stabilization. Furthermore the Somatomedin B domain can also interact with the urokinase plasminogen activator receptor (uPAR). Vitronectin-uPAR interaction is required and sufficient to initiate downstream changes in cell morphology migration and signal transduction. High plasma levels of both PAI-1 and uPAR have been shown to correlate with a negative prognosis for cancer patients. Additionally vitronectin is a component of platelets and is as such involved in hemostasis. Amino acid 45-47 (RGD) are capable of binding to membrane bound integrins which serve to anchor cells to the extracellular matrix. Vitronectin in plasma is an inactive monomer form. In contrast tissue vitronectin is an active multimeric form and is able to interact with various matrix ligands like proteoglycans and collagen. Mice with a genetic deletion of vitronectin show delayed wound healing suggesting an important role of vitronectin in tissue remodeling after injury. The monoclonal antibody BV1 binds to soluble vitronectin as well as to membrane bound vitronectin.

Somatomedin B is a growth hormone-dependent serum factor with protease-inhibiting activity.

Secreted extracellular space.

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.

N- and O-glycosylated (By similarity).

It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Contains 1 SMB (somatomedin B) domain. [1] Venter J. C. Adams M. D. Myers E. W. Li P. W. Mural R. J. Sutton G. G. Smith H. O. Yandell M. Evans C. A. Holt R. A. et al. The sequence of the human genome[2] Mural R. J. Istrail S. Sutton G. Florea L. Halpern A. L. Mobarry C. M. Lippert R. Walenz B. Shatkay H. Dew I. et al. Direct Submission[3] Suzuki S. Oldberg A. Hayman E. G. Pierschbacher M. D. Ruoslahti E. Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. [4] Suzuki S. Oldberg A. Hayman E. G. Pierschbacher M. D. Ruoslahti E. Submitted (JUN-1986) to the PIR data bank. [5] Jenne D. E. Stanley K. K. Molecular cloning of S-protein a link between complement coagulation and cell-substrate adhesion. [6] Jenne D. E. Stanley K. K. Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the \' pexin\' family and a model for their evolution. [7] Rieder M. J. Carrington D. P. Chung M. -W. Lee K. L. Poel C. L. Yi Q. Nickerson D. A. SeattleSNPs. NHLBI HL66682 program for genomic applications UW-FHCRC Seattle WA (URL: http://pga. gs. washington. edu). [8] Fryklund L. Sievertsson H. Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity. [9] Sigurdardottir O. Wiman B. Identification of a PAI-1 binding site in vitronectin. [10] Yaoi Y. Hashimoto K. Takahara K. Kato I. Insulin binds to type V collagen with retention of mitogenic activity.