|Calculated MW||77505 Da|
|Other Names||Protein kinase C delta type, Tyrosine-protein kinase PRKCD, nPKC-delta, Protein kinase C delta type regulatory subunit, Protein kinase C delta type catalytic subunit, Sphingosine-dependent protein kinase-1, SDK1, PRKCD|
|Target/Specificity||A phospho-specific peptide corresponding to residues surrounding Threonine 507 of human PKC delta was used as an immunogen. This antibody detects PKC delta phosphorylated at T507.|
|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||PKC delta Antibody Phospho (pT507) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor- initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self- antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)- induced inhibition of cell cycle progression at G1/S phase by up- regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro- survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl- phenylalanine (fMLP)-treated cells, is required for NCF1 (p47- phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C- terminal and regulates the interaction between MUC1 and beta- catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462).|
|Cellular Location||Cytoplasm Cytoplasm, perinuclear region. Nucleus. Cell membrane; Peripheral membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
PKC-delta has a biological activity which is closely related to Pkc1, and PKC-delta activates the Pkc1-mediated pathway through an activation of the Bck1 kinase. PKC-delta appears to play a critical role in growth control of yeast and mammalian cells. Suppression experiments suggest that PKC-delta desensitizes the pathway by regulating an aspect of G protein function (1). PKC-delta phosphorylates hRad9 in vitro and in cells exposed to genotoxic agents. It has been shown that PKC-delta is required for binding of hRad9 to Bcl-2. In concert with these results, inhibition of PKC-delta attenuates Rad9-mediated apoptosis. These findings demonstrate that PKC-delta is responsible for the regulation of Rad9 in the Hus1-Rad1 complex and in the apoptotic response to DNA damage (2). It has been reported a mechanism for the regulation of peripheral B-cell survival by serine/threonine protein kinase Cdelta (PKC-delta): spontaneous death of resting B cells is regulated by nuclear localization of PKC-delta that contributes to phosphorylation of histone H2B at serine 14 (S14-H2B) (3).
1. Nomoto S, et al. Genes Cells 2(10):601-14, 1997
2. Yoshida K, et al. EMBO J 22(6):1431-41, 2003
3. Mecklenbrauker I, et al. Nature 431(7007), 2004
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