产品名称
Monoclonal Anti-Vitronectin antibody produced in mouse, clone VIT-2, ascites fluid
biological source
mouse
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
Quality Level
Gene Information
human ... VTN(7448)
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
By immunoblotting, the product shows no cross-reactivity with fibronectin, laminin, merosin, collagen type IV or chondroitin sulfate types A, B and C.
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.
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.
Immunogen
human plasma vitronectin
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
Ovarian cancer ascites-derived vitronectin and fibronectin: Combined purification, molecular features and effects on cell response
Carduner L, et al.
Biochim. Biophys. Acta Gen. Subj., 1830(10), 4885-4897 (2013)
L Bello et al.
Neurosurgery, 49(2), 380-389 (2001-08-16)
This study analyzed the expression of integrins alpha(v)beta3 and alpha(v)beta5 in glioma tissue and focused on the periphery of high-grade gliomas. The analysis was performed with Western blot, immunohistochemistry, and immunofluorescence, by use of two monoclonal antibodies able to recognize
Novel purification of vitronectin from human plasma by heparin affinity chromatography
Yatohgo T, et al.
Cell Structure and Function, 13(4), 281-292 (1988)
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