17-294
Rho Activation Assay Kit
PP1/PP2A Toolbox for the selective in vitro dephosphorylation of proteins.
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About This Item
UNSPSC Code:
12161503
eCl@ss:
32161000
NACRES:
NA.84
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General description
A GST-tagged fusion protein, corresponding to residues 7-89 of mouse Rhotekin Rho Binding Domain, expressed in E. coli. Provided bound to glutathione-agarose. Purity >90%.
Application
PP1/PP2A Toolbox for the selective in vitro dephosphorylation of proteins.
Packaging
Kit capacity: 30 assays
Components
100X GTPγS, 10mM (Cat.# 20-176)
100X GDP, 100mM (Cat.# 20-177)
Mg2+ Lysis/Wash Buffer, 5X (Cat.# 20-168)
Anti-Rho (-A, -B, -C), clone 55 (Cat.# 05-778)
Rho Assay Reagent (Rhotekin RBD, agarose) (Cat.# 14-383)
100X GDP, 100mM (Cat.# 20-177)
Mg2+ Lysis/Wash Buffer, 5X (Cat.# 20-168)
Anti-Rho (-A, -B, -C), clone 55 (Cat.# 05-778)
Rho Assay Reagent (Rhotekin RBD, agarose) (Cat.# 14-383)
Quality
Routinely evaluated by precipitating GTP- Rho from 3T3/A31 cell lysates, subsequent detection by immunoblot analysis using anti-Rho (05-778).
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Aquatic Acute 1 - Aquatic Chronic 2 - Eye Dam. 1
Storage Class Code
10 - Combustible liquids
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Geraldine Pawlak et al.
The Journal of biological chemistry, 277(30), 26927-26933 (2002-05-16)
Cellular transformation by v-Src is believed to be caused by aberrant activation of signaling pathways that are normally regulated by cellular Src. Using normal rat kidney cells expressing a temperature-sensitive mutant of v-Src, we examined the role of the Raf/MEK/ERK
Jeanne M Manganello et al.
The Journal of biological chemistry, 278(1), 124-130 (2002-10-26)
The present studies mapped the protein kinase A (PKA) phosphorylation site of Galpha(13) and studied the consequences of its phosphorylation. Initial experiments using purified human Galpha(13) and the PKA catalytic subunit established that PKA directly phosphorylates Galpha(13). The location of
Toshifumi Sugatani et al.
The Journal of biological chemistry, 278(7), 5001-5008 (2002-12-04)
PTEN (also known as MMAC-1 or TEP-1) is a frequently mutated tumor suppressor gene in human cancer. PTEN functions have been identified in the regulation of cell survival, growth, adhesion, migration, and invasiveness. Here, we characterize the diverse signaling networks
M P Gratacap et al.
The Journal of biological chemistry, 276(51), 47906-47913 (2001-09-19)
Platelets were used to study the activation of Rho and Rac through G-protein-coupled receptors and its regulation by cyclic nucleotides. The thromboxane A(2) (TXA(2)) mimetic rapidly activated both small GTPases independently of integrin alpha(IIb)beta(3) activation., which leads to the activation
Johanna Liebl et al.
The Journal of biological chemistry, 285(46), 35932-35943 (2010-09-10)
Angiogenesis contributes to various pathological conditions. Due to the resistance against existing antiangiogenic therapy, an urgent need exists to understand the molecular basis of vessel growth and to identify new targets for antiangiogenic therapy. Here we show that cyclin-dependent kinase
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