The PKA RIIalpha (PRKAR2A) Monoclonal Antibody (CAB3889) is a high-quality antibody developed for reliable detection and analysis of target proteins. 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).
This antibody is validated for use in WB, ELISA applications and has demonstrated reactivity against Human samples.
Product Name:
PKA RIIalpha (PRKAR2A) Monoclonal Antibody
SKU:
CAB3889
Size:
100μL, 20μL
Reactivity:
Human
Clone Number:
ARC0860
Conjugate:
Unconjugated
Immunogen:
Recombinant protein (or fragment).This information is considered to be commercially sensitive.
Tested Applications:
WBELISA
Recommended Dilution:
WB
1:500 - 1:1000
ELISA
Recommended starting concentration is 1 μg/mL. Please optimize the concentration based on your specific assay requirements.
Synonyms:
PKR2, PKA RIIα (PRKAR2A)
Positive Sample:
HeLa, Hep G2
Cellular Localization:
Cell Membrane, Cytoplasm.
Calculated MW:
46kDa
Observed MW:
50kDa
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).
Purification Method
Affinity purification
Gene ID
5576
RRID
AB_2863154
Buffer Information
Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS containing 50% glycerol and 0.05% BSA, preserved with proclin300 or sodium azide, pH 7.3.
Western blot analysis of various lysates using PKA RIIα (PRKAR2A) Rabbit mAb (CAB3889) at 1:1000 dilution. Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25μg per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (AbGn00020). Exposure time: 3s.
