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Phospho-PI3 Kinase p85 (Tyr458)/p55 (Tyr199) Antibody

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品牌：CST/賽信通

貨號：4228T

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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 4228T Phospho-PI3 Kinase p85(Tyr458)/p55(Tyr199) Antibody 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：989

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, IP
Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110alpha, p110beta, p110gamma, and p110delta) have been isolated, and the regulatory subunits that associate with p110alpha, p110beta, and p110delta are p85alpha and p85beta (3). In contrast, p110gamma associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110gamma is activated by betagamma subunits of heterotrimeric G proteins (4).Protein extracts from 3T3-Src cells were profiled by PhosphoScan to identify phosphotyrosine peptides. Tyr458 of PI3K p85 and Tyr199 of PI3K p55 were among 180 phosphopeptides and 185 phosphotyrosine sites identified (5).

Supporting Data

REACTIVITY	M
SENSITIVITY	Endogenous
MW (kDa)	60 and 85
SOURCE	Rabbit

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
Immunoprecipitation	1:50

Storage

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

Specificity / Sensitivity

Phospho-PI3 Kinase p85 (Tyr458)/p55 (Tyr199) Antibody detects endogenous levels of p85/p55 only when phosphorylated at Tyr458/Tyr199.

Species Reactivity:

Mouse

Species predicted to react based on 100% sequence homology:

Human

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr458 of mouse p85. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP₂). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

Protein extracts from 3T3-Src cells were profiled by PhosphoScan? to identify phosphotyrosine peptides. Tyr458 of PI3K p85 and Tyr199 of PI3K p55 were among 180 phosphopeptides and 185 phosphotyrosine sites identified (5).

Cantley, L.C. (2002) Science 296, 1655-7.
Simpson, L. and Parsons, R. (2001) Exp Cell Res 264, 29-41.
Neri, L.M. et al. (2002) Biochim Biophys Acta 1584, 73-80.
Stoyanov, B. et al. (1995) Science 269, 690-3.
Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.