PRKAR2A Antilichaam, KO gevalideerd

CAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme 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 have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER) .

5576

P13861

Human, Mouse, Rat

Recombinant fusion protein containing a sequence corresponding to amino acids 1-404 of human PRKAR2A (NP_004148.1) .

Unconjugated

Primary Antibodies

Antibody is Knockout validated.

Apoptosis, Cancer, Cell Cycle, Neuroscience, Signal Transduction

Affinity purification

HeLa

Batch dependent

PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

None

Blue Ice

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

Observed: 46kDa

IgG

WB: 1:1000 - 1:2000

PRKAR2A

Jurkat

SW480

LO2

Mouse lung

Rat skeletal muscle

Protein kinase cAMP-dependent type II regulatory subunit alpha

Homo sapiens

PKR2, PRKAR2, cAMP-dependent protein kinase type II-alpha regulatory subunit, cAMP-dependent protein kinase regulatory subunit RII alpha, protein kinase A, RII-alpha subunit, protein kinase, cAMP-dependent, regulatory subunit type II alpha

WB

Liquid