Product Name
PKD1/2/3/PKC u, Polyclonal Antibody
Full Product Name
PKD1/2/3/PKC u (Phospho-Ser738/742) Antibody
Product Synonym Names
PKD, PKCM, PRKCM, PKC-MU
Product Gene Name
anti-PKD1/2/3/PKC u antibody
[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
3D Structure
ModBase 3D Structure for Q15139
Species Reactivity
Human, Mouse, Rat
Specificity
The antibody detects endogenous level of PKD1/2/3/PKC mu only when phosphorylated at Serine 738/742.
Purity/Purification
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy usi
Form/Format
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Concentration
1.0 mg/ml (lot specific)
Immunogen Type
Peptide-KLH
Immunogen Description
Peptide sequence around phosphorylation site of Serine738/Serine 742
Modification
Phospho-Ser738/742
Target Name
PKD1/2/3/PKC mu
Preparation and Storage
Store at -20 degree C/1 year
Other Notes
Small volumes of anti-PKD1/2/3/PKC u antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-PKD1/2/3/PKC u 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 morphogenic 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.
Product Categories/Family for anti-PKD1/2/3/PKC u antibody
Phospho-specific Ab
Applications Tested/Suitable for anti-PKD1/2/3/PKC u antibody
Western Blot (WB)
Application Notes for anti-PKD1/2/3/PKC u antibody
Western blotting: 1:500~1:1000
Western Blot (WB) of anti-PKD1/2/3/PKC u antibody
Western blot analysis of extracts from A549 cells with PMA using PKD1/2/3/PKC mu (Phospho-Ser738+Ser742) Antibody.The lane on the left is treated with the antigen-specific peptide.

NCBI/Uniprot data below describe general gene information for PKD1/2/3/PKC u. It may not necessarily be applicable to this product.
NCBI Accession #
NP_002733.2
[Other Products]
NCBI GenBank Nucleotide #
NM_002742.2
[Other Products]
UniProt Primary Accession #
Q15139
[Other Products]
UniProt Secondary Accession #
A6NL64; B2RAF6[Other Products]
UniProt Related Accession #
Q15139[Other Products]
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??[Similar Products]
NCBI Official Synonym Symbols
PKD; PKCM; PRKCM; PKC-MU
??[Similar Products]
NCBI Protein Information
serine/threonine-protein kinase D1
UniProt Protein Name
Serine/threonine-protein kinase D1
UniProt Synonym Protein Names
Protein kinase C mu type; Protein kinase D; nPKC-D1; nPKC-mu
UniProt Gene Name
PRKD1??[Similar Products]
UniProt Synonym Gene Names
PKD; PKD1; PRKCM??[Similar Products]
UniProt Entry Name
KPCD1_HUMAN
NCBI Summary for PKD1/2/3/PKC u
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 Comments for PKD1/2/3/PKC u
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: Protein kinase, CAMK; EC 2.7.11.13; Kinase, protein; Motility/polarity/chemotaxis; Protein kinase, Ser/Thr (non-receptor); Autophagy; CAMK group; PKD family
Chromosomal Location of Human Ortholog: 14q11
Cellular Component: integral to plasma membrane; cytoplasm; plasma membrane; trans-Golgi network; cell cortex; intercellular junction; 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; positive regulation of I-kappaB kinase/NF-kappaB cascade; sphingolipid metabolic process; sphingolipid biosynthetic process; apoptosis; negative regulation of endocytosis; protein amino acid autophosphorylation; 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; positive regulation of osteoblast differentiation; cell proliferation; peptidyl-serine phosphorylation; positive regulation of angiogenesis; innate immune response; positive regulation of endothelial cell proliferation; positive regulation of transcription from RNA polymerase II promoter; angiogenesis; vascular endothelial growth factor receptor signaling pathway; inflammatory response; Golgi organization and biogenesis
Research Articles on PKD1/2/3/PKC u
1. a positive relationship between L1 and pPKD1 in both cultured cerebellar neurons and human cerebellar tissue, suggesting that L1 functions in the modulation of PKD1 phosphorylation.
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