P7679
Monoclonal Anti-Platelet-Derived Growth Factor Receptor β antibody produced in mouse
clone PDGFR-B2, ascites fluid
Synonyme(s) :
Anti-PDGF Rβ
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About This Item
Numéro MDL:
Code UNSPSC :
51111800
Source biologique
mouse
Conjugué
unconjugated
Forme d'anticorps
ascites fluid
Clone
PDGFR-B2, monoclonal
Contient
15 mM sodium azide
Espèces réactives
human, pig
Technique(s)
immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 1:100 using denatured, non-reduced porcine uterus extract
Isotype
IgG2b
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
human ... PDGFRB(5159)
Spécificité
The antibody recognizes human and pig PDGF Rβ, but not mouse or rat. It can be used for immunoperoxidase and immunofluorescence staining of unfixed or acetone-fixed frozen tissue. The antibody induces clustering and down-regulation of PDGF Rβ. The antibody does not cross react with PDGF Rα.
Immunogène
PDGF β-receptor from pig uterus.
Clause de non-responsabilité
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.
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Mikhail Sergeev et al.
Biophysical journal, 91(10), 3884-3896 (2006-08-29)
We present higher-order moment analysis of fluorescence intensity fluctuations from individual laser scanning microscopy images applied to study monomer-oligomer distributions. We demonstrate that the number densities and brightness ratios of a mixed population of monomers and oligomers can be determined
Jonathan W D Comeau et al.
Biophysical journal, 91(12), 4611-4622 (2006-10-03)
Biomolecular interactions are fundamental to the vast majority of cellular processes, and identification of the major interacting components is usually the first step toward an understanding of the mechanisms that govern various cell functions. Thus, statistical image analyses that can
A Sorkin et al.
The Journal of cell biology, 112(3), 469-478 (1991-02-01)
The complementary DNAs for wildtype and tyrosine kinase-inactivated (K634A) forms of the PDGF beta-receptor were expressed in porcine aortic endothelial cells. We examined the internalization and degradation of ligands and receptors after exposure of receptor expressing cells to PDGF-BB, which
C Reuterdahl et al.
Laboratory investigation; a journal of technical methods and pathology, 64(3), 321-329 (1991-03-01)
Platelet-derived growth factor (PDGF) beta-receptor expression in normal and rheumatoid synovia was investigated by double immunofluorescence staining of frozen sections and by in situ hybridization. In the inflamed synovia, PDGF beta-receptor mRNA was present in vascular cells, as well as
P Höddelius et al.
Bioscience reports, 20(2), 119-127 (2000-08-31)
When the receptors for platelet-derived growth factor (PDGF) are activated they aggregate, become tyrosine-phosphorylated and elicit a cascade of down-stream signals, including mobilization of Ca2+ from intra- and extracellular stores. Receptor mobility in the plane of the membrane is a
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