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Phospho-PDGF Receptor beta (Tyr740) (32A9) Rabbit mAb

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品牌：CST/賽信通

貨號：3168T

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商品名稱	規(guī)格	代理級別	價(jià)格	運(yùn)費(fèi)	供應(yīng)商	購買
CST 3168T Phospho-PDGF Receptor beta(Tyr740)(32A9) Rabbit mAb 交貨周期:部分現(xiàn)貨，期貨3-4周左右，優(yōu)質(zhì)售后	20μl	經(jīng)銷	登錄可見	-	上海優(yōu)寧維生物科技股份有限公司	- + 立即購買庫存：999

產(chǎn)品詳情

文獻(xiàn)引用

文獻(xiàn)圖片

實(shí)驗(yàn)數(shù)據(jù)

應(yīng)用：W
反應(yīng)性:H
Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor alpha (PDGFRalpha) and PDGF receptor beta (PDGFRbeta). PDGFRalpha and PDGFRbeta share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRalpha homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRbeta homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor alpha/beta binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRalpha and PDGFRbeta can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCgamma, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRbeta is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRbeta (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRbeta (7). Tyr740 is also required for PDGFRbeta-mediated PI3 kinase activation (8).

Supporting Data

REACTIVITY	M
SENSITIVITY	Endogenous
MW (kDa)	190
Source/Isotype	Rabbit IgG

Application Key:

W-Western
IP-Immunoprecipitation
IHC-Immunohistochemistry
ChIP-Chromatin Immunoprecipitation
IF-Immunofluorescence
F-Flow Cytometry
E-P-ELISA-Peptide

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat
Hm-Hamster
Mk-Monkey
Vir-Virus
Mi-Mink
C-Chicken
Dm-D. melanogaster
X-Xenopus
Z-Zebrafish
B-Bovine
Dg-Dog
Pg-Pig
Sc-S. cerevisiae
Ce-C. elegans
Hr-Horse
All-All Species Expected

Product Usage Information

Application	Dilution
Western Blotting	1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-PDGF Receptor β (Tyr740) (32A9) Rabbit mAb detects endogenous levels of PDGF receptor β only when phosphorylated at tyrosine 740. The antibody may cross-react with activated PDGF receptor α.

Species Reactivity:

Mouse

Species predicted to react based on 100% sequence homology:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr740 of human PDGF receptor β.

Background

Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

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