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PKAc gamma, Active

Recombinant full-length human PKAcgamma was expressed by baculovirus in Sf9 insect cells using a N-terminal GST tag.
Catalog No. P53-10G


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Catalog No. Pack Size Price (USD)
P53-10G-05 5 ug $226
P53-10G-10 10 ug $325
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Overview:

PKA C-gamma (PKAcγ) is a third isoform of the catalytic subunit of cAMP-dependent protein kinase. It was isolated from a human testis cDNA library and was clearly derived from a gene distinct from C-alpha and C-beta and showed tissue-specific expression. Whereas at the amino acid level C-alpha and C-beta showed 93% homology, C-gamma showed only about 80% homology to both C-alpha and C-beta (1). The PRKACG gene is intronless, contains remnants of a poly(A) tail, is flanked by direct repeats, and is co-linear with the PRKACA gene(2).


Gene Aliases:

KAPG; PKAr; cAPKr; PRKACG


Genbank Number:


References:


1. Beebe, S. J. et al: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Molec. Endocr. 4: 465-475, 1990.

2. Reinton, N. et al: The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon. Genomics 49: 290-297, 1998.


Specific Activity:

Sample Kinase Activity Plot. For specific information on a given lot, see related technical data sheet.


Purity:

Sample Purity Data. For specific information on a given lot, see related technical data sheet.


Storage, Stability and Shipping:

Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.


Molecular Weight:

~65 kDa



 A. Hilton Benjamin et al., ATR Plays a Direct Antiapoptotic Role at Mitochondria, which Is Regulated by Prolyl Isomerase Pin1 Molecular Cell October 2015 10.1016/j.molcel.2015.08.008

 Fukuda Koichi et al., The Pseudoactive Site of ILK Is Essential for Its Binding to ?-Parvin and Localization to Focal Adhesions Molecular Cell December 2009 10.1016/j.molcel.2009.11.028

 A Thorne Curtis et al., Small-molecule inhibition of Wnt signaling through activation of casein kinase 1α Nature Chemical Biology November 2010 10.1038/nchembio.453

 GiovannaDi Nardo,AndreaBandino,InesBarone RobertaBaravalle et al., Impact of R264C and R264H polymorphisms in human aromatase function J Steroid Biochem Mol Biol.? October 2001 10.1016/j.jsbmb.2016.09.022

 Graczyk Agnieszka et al., S100A6 Competes with the TAZ2 Domain of p300 for Binding to p53 and Attenuates p53 Acetylation Journal of Molecular Biology September 2013 10.1016/j.jmb.2013.06.007

 Yamaguchi Fuminori et al., S100 Proteins Modulate Protein Phosphatase 5 FunctionA LINK BETWEEN CA2+ SIGNAL TRANSDUCTION AND PROTEIN DEPHOSPHORYLATION Journal of Biological Chemistry April 2012 10.1074/jbc.M111.329771

 S Shah et al., Regulation of FcRγ function by site-specific serine phosphorylation. Journal of Leukocyte Biology September 2016 10.1189/jlb.2AB0516-228R

 Martic? Sanela et al., Electrochemical investigations into Tau protein phosphorylations Analyst March 2012 10.1039/c2an35097a

 J. Coultrap Steven et al., Improving a Natural CaMKII Inhibitor by Random and Rational Design PLoS One October 2011 10.1371/journal.pone.0025245

 S Mondal et al., A bioluminescent assay for monitoring conjugation of ubiquitin and ubiquitin-like proteins. Analytical Biochemistry October 2016 10.1016/j.ab.2016.06.016

 Bhandaria Deepali et al., Cyclin-dependent kinase 5 activates guanine nucleotide exchange factor GIV/Girdin to orchestrate migration?proliferation dichotomy PNAS July 2015 10.1073/pnas.1514157112


RESEARCH AREAS

Apoptosis/Autophagy, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, NfkB Pathway, PKA/PKC Pathway, Ser/Thr Kinases


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