Anti-PKA C-alpha Mouse mAb

PTM BIO

Anti-PKA C-alpha Mouse mAb

5

Western Blot, ImmunoHistoChemistry Paraffin

WB, IHC-P

Research Use Only

Monoclonal

10200

Unconjugated

Mouse

IgG

cAMP-dependent protein kinase catalytic subunit alpha

The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls manycellular mechanisms such as gene transcription, ion transport, and protein Phosphorylatedrylation. Inactive PKA is a heterotetramer composed of aregulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits blockthe active sites on the C subunits. Three C subunit isoforms (C-alfa, C-bèta, and C-gamma) and two families of regulatory subunits (RI and RII) withdistinct cAMP binding properties have been identified. The two R families exist in two isoforms, alfaand bèta (RI-alfa, RI-bèta, RII-alfa, and RII-bèta). Uponbinding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substratespecificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the Phosphorylatedrylated serine or threonineresidue. Substrates that present this consensus sequence and have been shown to be Phosphorylatedrylated by PKA are Bad (Ser155), CREB(Ser133), and GSK-3 (GSK-3alfa Ser21 and GSK-3bèta Ser9). In addition, combined knock-down of PKA C-alfaand -bèta blocks cAMP-mediatedPhosphorylatedrylation of Raf (Ser43 and Ser259). AutoPhosphorylatedrylation and Phosphorylatedrylation by PDK-1 are two known mechanisms responsible forPhosphorylatedrylation of the C subunit at Thr197.

Stable for 12 months from date of receipt/reconstitution.

Human, Mouse

Human, Mouse

Protein A purified

Store at -20°C. Avoid freeze/thaw cycles.

12352203