Rabbit anti-Human PKD1/PKC mu Polyclonal Antibody | anti-PKD1/PKCmu antibody

PKD1/PKC mu Antibody

Cat. Num. AAA9613864

• Gene Names: PRKD1; PKD; PKCM; PRKCM; PKC-MU
• Reactivity: Human
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin
• Synonyms: PKD1/PKC mu; Polyclonal Antibody; PKD1/PKC mu Antibody; KPCD1_HUMAN; nPKC D1; nPKC mu; nPKC-D1; nPKC-mu; nPKCD1; nPKCmu; PKC; PKC MU; PKCM; PKCmu; PKD 1; PKD; PKD1; PRKCM; PRKD 1; Prkd1; Protein kinase C mu; Protein kinase C mu type; Protein kinase D; Protein kinase D1; Serine/threonine protein kinase D1; Serine/threonine-protein kinase D1; anti-PKD1/PKCmu antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: PKD1/PKC mu Antibody detects endogenous levels of total PKD1/PKC mu.
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-PKD1/PKCmu antibody: Peptide ELISA (EIA)
• Application Notes: Peptide ELISA: 1:20,000-1:40,000
• Immunogen: A synthesized peptide derived from human PKD1/PKC mu.
• Conjugation: Unconjugated
• Fragment: Fab fragment
• Post Translational Modifications: Phosphorylated at Ser-397 and Ser-401 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated at Tyr-95 and by ABL at Tyr-463, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-738/Ser-742 by PKRD. Phosphorylated on Ser-910 upon S.enterica infection in macrophages (By similarity).
• Subunit Structure: Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13. Interacts with DAPK1 in an oxidative stress-regulated manner. Interacts with USP28; the interaction induces phosphorylation of USP28 and activated KRAS-mediated stabilization of ZNF304. Interacts with AKAP13 (via C-terminal domain) (By similarity).
• Similarity: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.
• Subcellular Location: Cytoplasm. Cell membrane. Golgi apparatus>trans-Golgi network.; Note: Translocation to the cell membrane is required for kinase activation.
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Related Product Information for anti-PKD1/PKCmu antibody

Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells. Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (By similarity).

NCBI and Uniprot Product Information

• NCBI GI #: 115529463
• NCBI GeneID: 5587
• NCBI Accession #: NP_002733.2
• NCBI GenBank Nucleotide #: NM_002742.2
• UniProt Accession #: Q15139; A6NL64; B2RAF6
• Molecular Weight: 101,704 Da
• NCBI Official Full Name: serine/threonine-protein kinase D1
• NCBI Official Synonym Full Names: protein kinase D1
• NCBI Official Symbol: PRKD1
• NCBI Official Synonym Symbols: PKD; PKCM; PRKCM; PKC-MU
• NCBI Protein Information: serine/threonine-protein kinase D1; nPKC-D1; nPKC-mu; protein kinase C, mu; protein kinase C mu type
• UniProt Protein Name: Serine/threonine-protein kinase D1
• UniProt Gene Name: PRKD1
• UniProt Synonym Gene Names: PKD; PKD1; PRKCM
• UniProt Entry Name: KPCD1_HUMAN

NCBI Description

PRKD1 is a serine/threonine kinase that regulates a variety of cellular functions, including membrane receptor signaling, transport at the Golgi, protection from oxidative stress at the mitochondria, gene transcription, and regulation of cell shape, motility, and adhesion (summary by Eiseler et al., 2009 [PubMed 19329994]).[supplied by OMIM, Nov 2010]

Uniprot Description

PRKD1: a CAMK kinase of the PKD family. Cleavage by caspase-3 following DNA damage activates it and alters its subcellular localization. Sensitizes cells to apoptosis induced by genotoxic stress. Its cleavage is blocked in cells that over-express the anti-apoptotic Bcl-x(L) protein. Expression of a caspase-resistant mutant partially inhibits DNA damage-induced apoptosis. Its activation by TLR ligands is dependent on MyD88, IRAK4 and -1, but not TRAF6. Essential for MyD88-dependent proinflammatory immune responses. Activated by diacylglycerol and phorbol esters. Binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface. Colocalizes with F-actin at peripheral F-actin-rich structures in membrane ruffles at the edge of lamellipodia in cervical carcinoma cells. Substrates reportedly include critical regulatory proteins including CREB, SSH1L, CTNNB1, HDACs 5 and 7, PKD1, HPK1, MARK2, PIP5K2A, PPP1R14A

Protein type: Kinase, protein; Autophagy; Protein kinase, CAMK; Protein kinase, Ser/Thr (non-receptor); Motility/polarity/chemotaxis; EC 2.7.11.13; CAMK group; PKD family

Chromosomal Location of Human Ortholog: 14q11

Cellular Component: integral to plasma membrane; cytoplasm; plasma membrane; intercellular junction; trans-Golgi network; cell cortex; nucleus; cytosol

Molecular Function: identical protein binding; protein serine/threonine kinase activity; protein binding; protein kinase C activity; metal ion binding; ATP binding

Biological Process: integrin-mediated signaling pathway; sphingolipid metabolic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; sphingolipid biosynthetic process; apoptosis; protein amino acid autophosphorylation; negative regulation of endocytosis; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; signal transduction; positive regulation of peptidyl-serine phosphorylation; activation of NF-kappaB transcription factor; Golgi vesicle transport; cell proliferation; positive regulation of osteoblast differentiation; peptidyl-serine phosphorylation; positive regulation of angiogenesis; innate immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; angiogenesis; vascular endothelial growth factor receptor signaling pathway; inflammatory response; Golgi organization and biogenesis