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Mouse Anti-VTN Recombinant Antibody (CBYCV-137) (CBMAB-V0116-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYCV-137
Antibody Isotype
IgG2b, Κ
Application
ELISA, WB

Basic Information

Immunogen
Human vitronectin purified from plasma by heparin-affinity chromatography
Specificity
Human
Antibody Isotype
IgG2b, Κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Vitronectin
Introduction
VTN is a member of the pexin family. It is found in serum and tissues and promotes cell adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, and binds to several serpin serine protease inhibitors. It is a secreted protein and exists in either a single chain form or a clipped, two chain form held together by a disulfide bond.
Entrez Gene ID
7448
UniProt ID
P04004
Alternative Names
Vitronectin; Serum Spreading Factor; Complement S-Protein; Somatomedin B; S-Protein; V75
Function
Vitronectin is a cell adhesion and spreading factor found in serum and tissues. 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.
Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
Biological Process
Biological Process cell adhesion Source:ProtInc1 Publication
Biological Process cell adhesion mediated by integrin Source:BHF-UCL1 Publication
Biological Process cell migration Source:UniProtKB1 Publication
Biological Process cell-matrix adhesion Source:BHF-UCL1 Publication
Biological Process endodermal cell differentiation Source:UniProtKB1 Publication
Biological Process extracellular matrix organization Source:Ensembl
Biological Process immune response Source:ProtInc1 Publication
Biological Process liver regeneration Source:Ensembl
Biological Process negative regulation of blood coagulation Source:BHF-UCL1 Publication
Biological Process negative regulation of endopeptidase activity Source:BHF-UCL1 Publication
Biological Process negative regulation of fibrinolysis Source:ComplexPortal1 Publication
Biological Process oligodendrocyte differentiation Source:Ensembl
Biological Process positive regulation of cell-substrate adhesion Source:Ensembl
Biological Process positive regulation of peptidyl-tyrosine phosphorylation Source:BHF-UCL1 Publication
Biological Process positive regulation of protein binding Source:BHF-UCL1 Publication
Biological Process positive regulation of receptor-mediated endocytosis Source:BHF-UCL1 Publication
Biological Process positive regulation of smooth muscle cell migration Source:BHF-UCL1 Publication
Biological Process positive regulation of vascular endothelial growth factor receptor signaling pathway Source:BHF-UCL1 Publication
Biological Process positive regulation of wound healing Source:BHF-UCL1 Publication
Biological Process protein polymerization Source:Ensembl
Biological Process regulation of cell adhesion Source:ComplexPortal1 Publication
Biological Process smooth muscle cell-matrix adhesion Source:BHF-UCL1 Publication
Cellular Location
Secreted, extracellular space
Parasitophorous vacuole
(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995).
Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995).
PTM
Sulfated on tyrosine residues.
N- and O-glycosylated.
Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.
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.
Phosphorylation sites are present in the extracellular medium.
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For research use only. Not intended for any clinical use.

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