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V7881

Sigma-Aldrich

Monoclonal Anti-Vitronectin antibody produced in mouse

clone VIT-2, ascites fluid

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MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

VIT-2, monoclonal

mol wt

antigen 65-75 kDa

contains

15 mM sodium azide

species reactivity

human

technique(s)

indirect ELISA: suitable
indirect immunofluorescence: suitable using human cultured fibroblasts
microarray: suitable
western blot: 1:2,500 using a denatured and reduced preparation of purified human plasma vitronectin

isotype

IgM

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... VTN(7448)

General description

Monoclonal Anti-Vitronectin (mouse IgM isotype) is derived from the VIT-2 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with purified human plasma vitronectin. Vitronectin is also referred as serum-spreading factor, S-protein of complement or epibolin. This monomeric acidic protein is one of the major multifunctional cell-adhesive glycoproteins in mammalian plasma and serum. This protein is usually seen as a mixture of 75 kDa and 65 kDa polypeptides. Human plasma and serum contain 0.1-0.4 mg/ml of vitronectin which is synthesized in the liver. It is also present in amniotic fluid and urine.

Specificity

By immunoblotting, the product shows no cross-reactivity with fibronectin, laminin, merosin, collagen type IV or chondroitin sulfate types A, B and C.

Immunogen

human plasma vitronectin

Application

Monoclonal Anti-Vitronectin antibody produced in mouse has been used in:
  • immunocytochemisry
  • western blotting
  • immunoprecipitation
  • immunofluorescence
  • enzyme-linked immunosorbent assay (ELISA)

Biochem/physiol Actions

Vitronectin binds to heparin, collagen, streptococci and variety of cultured cells. It also acts as an inhibitor of the complement cascade by binding to the C5b-9 complex. Vitronectin protects thrombin from inactivation by antithrombin III in the presence of heparin, binds and stabilizes the activity of plasminogen activator inhibitor and mediates many other physiological functions.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

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M Delannet et al.
Development (Cambridge, England), 120(9), 2687-2702 (1994-09-01)
To identify potentially important extracellular matrix adhesive molecules in neural crest cell migration, the possible role of vitronectin and its corresponding integrin receptors was examined in the adhesion and migration of avian neural crest cells in vitro. Adhesion and migration
S Cherian et al.
Neuropathology and applied neurobiology, 30(6), 585-600 (2004-11-16)
Posthaemorrhagic ventricular dilatation (PHVD) is a common complication of intraventricular haemorrhage in premature infants. The aim of this study was to investigate the role of transforming growth factor-betas (TGF-betas), a family of polypeptides with potent desmoplastic properties, in the aetiology
Novel purification of vitronectin from human plasma by heparin affinity chromatography
Yatohgo T, et al.
Cell Structure and Function, 13(4), 281-292 (1988)
Phenotypic characterization of human smooth muscle cells derived from atherosclerotic tibial and peroneal arteries
Jones BA, et al.
Journal of Vascular Surgery, 24(5), 883-891 (1996)
Hepatocyte Growth Factor Regulates E Box-Dependent Plasminogen Activator Inhibitor Type 1 Gene Expression in HepG2 Liver Cells
Imagawa S, et al.
Arteriosclerosis, Thrombosis, and Vascular Biology (2006)

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