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Merck
CN

17-300

Ral Activation Assay Kit

Non-radioactive Ral Activation Assay Kit can be used to precipitate Ral-A-GTP from cell lysates & detection by a Ral-A specific antibody.

别名:

Activation Assay Kit, Ral Assay Kit

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关于此项目

UNSPSC Code:
12161503
NACRES:
NA.84
eCl@ss:
32161000
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Quality Level

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable, affinity binding assay: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

Gene Information

human ... RALA(5898)

Packaging

Kit capacity: 30 assays

Analysis Note

Routinely evaluated by affinity precipitation/immunoblot analysis. Ral-A-GTP was precipitated from EGF-stimulated Cos-7 cell lysates. The precipitated Ral-A-GTP was detected by Western immunoblot analysis using anti-Ral A.

Other Notes

Ral Activation Assay Buffer, 5X (Cat.# 20-196)

100X GTPγS, 10mM (Cat.# 20-176)

100X GDP, 100mM (Cat.# 20-177)

Anti-Ral-A

Ral Assay Reagent (Ral BP1, agarose) (Cat.# 14-415)

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.


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Corrosion

signalword

Danger

Hazard Classifications

Aquatic Chronic 3 - ED ENV 1 - Eye Dam. 1

存储类别

10 - Combustible liquids

wgk

WGK 3



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2'-Methylseleno-modified oligoribonucleotides for X-ray crystallography synthesized by the ACE RNA solid-phase approach.
Barbara Puffer,Holger Moroder,Michaela Aigner,Ronald Micura
Nucleic Acids Research null
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The FEBS journal, 281(13), 2977-2989 (2014-05-13)
Ral proteins are small GTPases that play critical roles in normal physiology and in oncogenesis. There is little information on the GTPase-activating proteins (GAPs) that downregulate their activity. Here, we provide evidence that the noncatalytic β subunit of RalGAPα1/2 β
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