Rabbit Anti-PRKCG Recombinant Antibody (BA0298) (CBMAB-0701CQ)

Rabbit

Human, Mouse, Rat

BA0298

IgG

WB

Synthetic peptide from residues in Human PKC Gamma

Human, Mouse, Rat

IgG

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

>95% as determined by analysis by SDS-PAGE

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Protein Kinase C Gamma

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. Protein kinase C (PKC) refers to a family of serine/threonine protein kinases grouped by their activation mechanism. Conventional PKCs (cPKC alpha-, betaI- , betaII- and gamma-) are activated by phosphatidylserine in a calcium dependent manner and can bind diacylglycerol.

PKCC; PKCG; SCA14; PKC-gamma

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity).
Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity).

Chemical synaptic transmissionIEA:Ensembl
Chemosensory behaviorIEA:Ensembl
InnervationIEA:Ensembl
Intracellular signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Learning or memoryIEA:Ensembl
Long-term synaptic potentiationIEA:Ensembl
Negative regulation of neuron apoptotic processISS:UniProtKB
Negative regulation of proteasomal protein catabolic processISS:UniProtKB
Negative regulation of protein catabolic processManual Assertion Based On ExperimentIDA:HGNC-UCL
Negative regulation of protein ubiquitinationManual Assertion Based On ExperimentIDA:HGNC-UCL
Peptidyl-serine phosphorylationManual Assertion Based On ExperimentIBA:GO_Central
PhosphorylationManual Assertion Based On ExperimentIDA:HGNC-UCL
Positive regulation of mismatch repairManual Assertion Based On ExperimentIDA:HGNC-UCL
Presynaptic modulation of chemical synaptic transmissionIEA:Ensembl
Protein autophosphorylationIEA:Ensembl
Protein phosphorylationManual Assertion Based On ExperimentTAS:ProtInc
Regulation of circadian rhythmISS:UniProtKB
Regulation of phagocytosisIEA:Ensembl
Regulation of response to foodISS:UniProtKB
Regulation of synaptic vesicle exocytosisIEA:Ensembl
Response to morphineISS:UniProtKB
Response to painISS:UniProtKB
Response to psychosocial stressIEA:Ensembl
Response to toxic substanceIEA:Ensembl
Rhythmic processIEA:UniProtKB-KW

Cytoplasm
Cytoplasm, perinuclear region
Cell membrane
Synapse, synaptosome
Cell projection, dendrite
Translocates to synaptic membranes on stimulation.

Spinocerebellar ataxia 14 (SCA14):
Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA).

Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.
Ubiquitinated.