CST, 3927S, PKA RI-alpha/beta Antibody

Polyclonal Antibody for studying PKAR1B/PRKAR1A. Validated for Western Blotting,Immunofluorescence (Immunocytochemistry). Highly specific and rigorously validated in-house, PKA RI-alpha/beta Antibody (CST #3927) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunofluorescence (Immunocytochemistry): 1:100 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 Available protocols: Western Blotting, Immunofluorescence (Immunocytochemistry) Specificity / Sensitivity PKA RI-alpha/beta Antibody detects endogenous levels of total PKA RI-α and PKA RI-β protein. Species Reactivity: Human, Mouse, Rat Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn310 of human PKA RI-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). Alternate Names ACRDYS1; ADOHR; cAMP-dependent protein kinase regulatory subunit RIalpha; cAMP-dependent protein kinase type I-alpha regulatory chain; cAMP-dependent protein kinase type I-alpha regulatory subunit; cAMP-dependent protein kinase type I-beta regulatory subunit; CAR; Carney complex type 1; CNC; CNC1; DKFZp779L0468; epididymis secretory sperm binding protein; KAP0; KAP1; MGC17251; PKAR1A; PKAR1B; PKR1; PPNAD1; PRKAR1; PRKAR1A; PRKAR1B; protein kinase A type 1a regulatory subunit; protein kinase cAMP-dependent type I regulatory subunit alpha; protein kinase cAMP-dependent type I regulatory subunit beta; protein kinase, cAMP-dependent, regulatory subunit type I alpha; protein kinase, cAMP-dependent, regulatory subunit type I beta; protein kinase, cAMP-dependent, regulatory, type I, alpha; protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1); protein kinase, cAMP-dependent, regulatory, type I, beta; Tissue-specific extinguisher 1; TSE1 Specification REACTIVITY: H M R SENSITIVITY: Endogenous MW (kDa): 48 SOURCE: Rabbit