- CITATIONS: 2
|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||40590 Da|
|Other Names||cAMP-dependent protein kinase catalytic subunit alpha, PKA C-alpha, PRKACA, PKACA|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human PKC C-alpha subunit was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PKA C Antibody alpha is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose- mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B- alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha- difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.|
|Cellular Location||Cytoplasm. Cell membrane. Nucleus. Mitochondrion. Membrane; Lipid-anchor. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity)|
|Tissue Location||Isoform 1 is ubiquitous. Isoform 2 is sperm- specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.|
Provided below are standard protocols that you may find useful for product applications.
PKA (or cAPK) is a cyclic AMP-dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, and gene transcription (1,2). PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C-alpha, C-beta, and C-gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states (2,3). C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Studies have shown the importance of PKA phosphorylation at Thr 197 regards to PKA maturation, optimal conformation, and catalytic activity (4, 5).
1. Montminy, M, Annu. Rev. Biochem. 66: 807
2. Beebe, SJ et al. Semin Cancer Biol. 5: 285
3. Braun RK et al. Arch Biochem Biophys. 289: 187
4. Moore, M.J. et al. (2002) J. Biol. Chem. 277, 47878-47884.
5. Feschenko MS, Sweadner KJ. J. Biol. Chem 269(48):30436-44, 1994
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