|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||40434 Da|
|Other Names||cAMP-dependent protein kinase catalytic subunit gamma, PKA C-gamma, PRKACG|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding threonine 197 of human PKA C-gamma was used as an immunogen. This antibody detects PKA C-gamma phosphorylated on thr197.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PKA-C Antibody (gamma) Phospho-pT197 is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphorylates a large number of substrates in the cytoplasm and the nucleus.|
|Tissue Location||Testis specific. But important tissues such as brain and ovary have not been analyzed for the content of transcript|
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Provided below are standard protocols that you may find useful for product applications.
PKA (or cAPK) is a cyclic AMP-dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, and gene transcription (1,2). PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C-alpha, C-beta, and C-gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states (2,3). C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue-specific expression of C gamma, suggests a pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP-dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits (4).
1. Montminy, M, Annu. Rev. Biochem. 66: 807-822 (1997).
2. Beebe, SJ et al. Semin Cancer Biol. 5: 285-94 (1994).
3. Braun RK et al. Arch Biochem Biophys. 289: 187-91 (1991).
4. Beebe SJ et al. Mol Endocrinol 4(3):465-75, 1990
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