Anti-PKA/Cγ (N-term) antibody produced in rabbit

NA.41

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. This protein, the gamma-catalytic subunit, is a member of the Ser/Thr protein kinase family. The gene is intronless and is thought to be a retrotransposon derived from the gene for the alpha form of the catalytic subunit.

PKA/C GAMMA (13-49)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human PKA/C.

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.

rabbit

unconjugated

IgG fraction of antiserum

primary antibodies

polyclonal

buffered aqueous solution

human

indirect ELISA: 1:1000
western blot: 1:100-1:500

NP_002723

P22612

dry ice

−20℃

human ... PRKACG(5568)

12 - Non Combustible Liquids

nwg