Quantity size:
0.2ml
Concentration:
1mg/ml 跨膜接头蛋白PAG抗体 Buffer = 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Background:
The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, 跨膜接头蛋白PAG抗体is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
跨膜接头蛋白PAG抗体Also known as:
CBP; Csk Binding Protein; Csk-binding protein; FLJ37858; MGC138364; PAG 1; PAG; PAG1; PAG1_HUMAN; Phosphoprotein associated with glycosphingolipid enriched microdomains 1; Phosphoprotein associated with glycosphingolipid enriched microdomains; Phosphoprotein associated with glycosphingolipid microdomains 1; Phosphoprotein associated with 跨膜接头蛋白PAG抗体glycosphingolipid-enriched microdomains 1; Protein Associated with Glycosphingolipid Enriched Microdomains; Transmembrane adapter protein PAG; Transmembrane phosphoprotein Cbp.
Specificity:
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Rabbit Polyclonal IgG, affinity purified by Protein A.
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Reacts with: Human, Mouse, Rat, Dog, Horse, Rabbit, .
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Immunogen: KLH conjugated synthetic peptide derived from human PAG1.
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Predicted Molecular Weight: 47kDa.
跨膜接头蛋白PAG抗体Storage:
Shipped at 4℃, Store at -20℃ (Avoid repeated freeze/thaw cycles).
Application:
WB=1:100-500 ELISA=1:500-1000 IHC-P=1:100-500 IHC-F=1:100-500 ICC=1:100-500 IF=1:100-500
Not yet tested in other applications.
Optimal working dilutions must be determined by the end user.
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