[KD Validated] PKA C-alpha (PRKACA) Mouse mAb,ABclonal,A18603

Reactivity

Human, Mouse, Rat

Application

WB, IF/ICC, ELISA

Platform ID

BAB445009495

ABclonal

Headquarters

500W Cummings Park, Ste. 6500 Woburn, MA 01801

Contact

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Product Specifications
Scientific Background

Specifications

Name[KD Validated] PKA C-alpha (PRKACA) Mouse mAb
Cat. No.A18603
RRID#N/A
IsotypeIgG2B,Kappa
ReactivityHuman, Mouse, Rat
ApplicationWB, IF/ICC, ELISA
Working DilutionsWB:1:10000 - 1:40000 | IF/ICC:1:50 - 1:200 | ELISA:Recommended starting concentration is 1 μg/mL. Please optimize the concentration based on your specific assay requirements.
Molecular Weight40kDa
ImmunogenRecombinant protein (or fragment).This information is considered to be commercially sensitive.
PurityAffinity purification
Appearance/FormLiquid
StorageStore at -20℃. Avoid freeze / thaw cycles.; Buffer: PBS containing 50% glycerol, preserved with proclin300 or sodium azide (as specified on the Certificate of Analysis), pH 7.3.
Regulatory StatusResearch Use Only

Scientific Background

This gene encodes one of the catalytic subunits of protein kinase A, which exists as a tetrameric holoenzyme with two regulatory subunits and two catalytic subunits, in its inactive form. 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. cAMP-dependent phosphorylation of proteins by protein kinase A is important to many cellular processes, including differentiation, proliferation, and apoptosis. Constitutive activation of this gene caused either by somatic mutations, or genomic duplications of regions that include this gene, have been associated with hyperplasias and adenomas of the adrenal cortex and are linked to corticotropin-independent Cushing's syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. Tissue-specific isoforms that differ at the N-terminus have been described, and these isoforms may differ in the post-translational modifications that occur at the N-terminus of some isoforms.

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