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PKA C-α Antibody

PKA C-α Antibody #4782

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Supporting Data

REACTIVITY	H M R
SENSITIVITY	Endogenous
MW (kDa)	42
SOURCE	Rabbit

Application Key:

WB-Western Blotting
IP-Immunoprecipitation
IF-Immunofluorescence
F-Flow Cytometry

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat

Product Information

Product Usage Information

Application	Dilution
Western Blotting	1:1000
Immunoprecipitation	1:50
Immunofluorescence (Immunocytochemistry)	1:50 - 1:100
Flow Cytometry (Fixed/Permeabilized)	1:50 - 1:200

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

PKA C-α Antibody detects endogenous levels of total PKA C-α.

Species Reactivity:

Human, Mouse, Rat

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminal sequence of human PKA C-α. Antibodies are purified by protein A and peptide affinity chromatography.

Background

The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).

Database Links

UniProt ID: P17612

Entrez-Gene Id: 5566

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