PKA alpha/beta CAT (Phospho-Thr197) Colorimetric Cell-Based ELISA Kit

• Description:

  The PKA alpha/beta CAT (Phospho-Thr197) Cell-Based ELISA Kit is a convenient, lysate-free, high throughput and sensitive assay kit that can monitor PKA alpha/beta CAT (Phospho-Thr197) protein expression profile in cells. The kit can be used for measuring the relative amounts of PKA alpha/beta CAT (Phospho-Thr197) in cultured cells as well as screening for the effects that various treatments, inhibitors (ie. siRNA or chemicals), or activators have on PKA alpha/beta CAT (Phospho-Thr197) .

• Synonyms:

  CAMP-dependent protein kinase catalytic subunit alpha; PKA C-alpha; PRKACA ; PKACA ; cAMP-dependent protein kinase catalytic subunit beta; PKA C-beta; PRKACB

• Gene Name:

  PRKACA

• UniProt:

  P17612

• Reactivity:

  Human, Mouse, Rat

• Tissue Specificity:

  Isoform 1 is ubiquitous. Isoform 2 is sperm- specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.

• Applications:

  ELISA

• Sample Type:

  Cell lines

• Detection Range:

  > 5000 cells/well

• 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. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490) .

• Molecular Weight:

  40590 MW

• Shipping Conditions:

  Available

• Storage Conditions:

  Store at 4°C for up to 6 months.

• Other Gene Names:

  CAMP-dependent protein kinase catalytic subunit alpha

• Subcellular Location:

  Cytoplasm. Cell membrane. Nucleus. Mitochondrion. Membrane; Lipid-anchor. 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) . Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat shock (PubMed:21085490) .