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Key Documents

P7746

Sigma-Aldrich

Anti-phospho-PAK1/2/3 (pThr423) antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.44

生物源

rabbit

品質等級

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous glycerol solution

物種活性

human

技術

western blot: 1:1,000 using His-tagged wild-type and S139A/T421A double mutant PAK3.

UniProt登錄號

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

phosphorylation (pThr423)

基因資訊

human ... PAK1(5058)

一般說明

p21-activated kinases are a family of highly conserved serine/threonine protein kinases that are activated by small GTPases of Cdc42 and Rac families. There are 2 groups of PAKs in mammals, group A and B. The group A members are three isoforms, PAK1, PAK2, and PAK3 (also known as α-PAK, γ-PAK, and β-PAK, respectively). PAKs are actively involved in regulation of MAPK pathways by phosphorylation of Raf-1 and MEK-1. They also regulate cytoskeletal reorganization by interaction with GTPases. Autophosphorylation of threonine 423 (threonine 402 for PAK2 and threonine 421 for PAK3), catalyzed by Cdc42, is required for activation of PAK.
The antibody detects human PAK1, PAK2 and PAK3, phosphorylated at Thr423. Other species with 100% PAK homology are expected to react.

免疫原

synthetic phosphopeptide derived from the region of PAK that contains threonine 423.

應用

A recommended working concentration of 0.1-1.0 μg/mL is determined by immunoblotting using Histagged wild-type and S139A/T421A double mutant PAK3.

外觀

Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


分析證明 (COA)

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Clemens Hofmann et al.
Journal of cell science, 117(Pt 19), 4343-4354 (2004-08-28)
p21-activated kinases (Paks) are a highly conserved family of enzymes that bind to and are activated by small GTPases of the Cdc42 and Rac families. With the notable exception of plants, nearly all eukaryotes encode one or more Pak genes
Giampiero Porcu et al.
Molecular cancer, 12(1), 88-88 (2013-08-07)
Farnesyltransferase inhibitors (FTIs) are anticancer agents with a spectrum of activity in Ras-dependent and independent tumor cellular and xenograph models. How inhibition of protein farnesylation by FTIs results in reduced cancer cell proliferation is poorly understood due to the multiplicity
Zhou-shen Zhao et al.
The Biochemical journal, 386(Pt 2), 201-214 (2004-11-19)
The Rho GTPases are a family of molecular switches that are critical regulators of signal transduction pathways in eukaryotic cells. They are known principally for their role in regulating the cytoskeleton, and do so by recruiting a variety of downstream
Christy C Ong et al.
Oncotarget, 2(6), 491-496 (2011-06-10)
The p21-activated kinases (PAKs) are central players in growth factor signaling networks and morphogenetic processes that control proliferation, cell polarity, invasion and actin cytoskeleton organization. This raises the possibility that interfering with PAK activity may produce significant anti-tumor activity. In
Mengwei Zang et al.
The Journal of biological chemistry, 277(6), 4395-4405 (2001-12-26)
Activation of Raf-1 is a complex process in which phosphorylation of Ser(338)-Tyr(341) is a critical step. Previous studies have shown that Pak1/2 is implicated in both Ras-dependent and -independent activation of Raf-1 by phosphorylating Raf Ser(338). The present study explores

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