PKC mu, Polyclonal Antibody

PKD; PKD1; PRKCM; Serine/threonine-protein kinase D1; Protein kinase C mu type; Protein kinase D; nPKC-D1; nPKC-mu

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Recognizes endogenous levels of PKC mu protein.

The antibody was purified by immunogen affinity chromatography.

Liquid in 0.42% Potassium Phosphate, 0.87% Sodium Chloride, pH 7.3, 30% Glycerol, and 0.01% Sodium Azide.

Shipped and store at 4 degree C for one year. Do not freeze.

Small volumes of anti-PRKD1 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.

Rabbit polyclonal antibody to PKC mu

Western Blot (WB), Immunohistochemistry (IHC)

Western Blot: (1/500 - 1/1000); Immunohistochemistry: (1/100 - 1/200)

Western blot analysis of PKC mu expression in HEK293T (A), Hela (B) whole cell lysates.

Immunohistochemical analysis of PKC mu staining in human breast cancer formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.

101,704 Da

protein kinase D1

serine/threonine-protein kinase D1

Serine/threonine-protein kinase D1

PKD; PKD1; PRKCM  [Similar Products]

KPCD1_HUMAN

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]

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

Chromosomal Location of Human Ortholog: 14q11

Cellular Component: cytoplasm; cytosol; Golgi apparatus; integral to plasma membrane; nucleus; plasma membrane; trans-Golgi network

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

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

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