兔抗PRKAR1A多克隆抗体

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. 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. 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). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197.

Applications:

WB

Name of antibody:

PRKAR1A

Immunogen:

Fusion protein of human PRKAR1A

Full name:

protein kinase, cAMP-dependent, regulatory, type I, alpha

Synonyms：

PRKAR1A; CAR; CNC; CNC1; DKFZp779L0468; MGC17251; PKR1; PPNAD1; PRKAR1; TSE1

SwissProt:

P10644

WB Predicted band size:

43 kDa

WB Positive control:

HeLa, CEM, A549, SW480, PC3, V251, HCTnb and heart tissue

WB Recommended dilution:

500-2000