Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

PKD2 (D1A7) Rabbit mAb #8188

Applications Reactivity Sensitivity MW (kDa) Isotype
W IF-IC H Mk Pg Endogenous 105 Rabbit IgG

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  Mk=Monkey  Pg=Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

PKD2 (D1A7) Rabbit mAb recognizes endogenous levels of total PKD2 protein. This antibody does not cross react with PKD1 or PKD3.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly491 of human PKD2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using PKD2 (D1A7) Rabbit mAb.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HT-1080 cells, serum starved (left) or treated with phorbol di-butyrate (PDBu) (100 nM for 15 min) using PKD2 (D1A7) Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

Background

Protein kinase D2 (PKD2) is one of three members of the protein kinase D family, including PKD1/PKCμ and PKD3/PKCν, that belong to the calcium/calmodulin superfamily of serine/threonine protein kinases (1,2). PKDs contain a conserved, carboxy-terminal catalytic domain, an amino-terminal regulatory region hallmarked by a PH domain that coordinates subcellular localization, and two zinc-finger/C1 lipid-binding domains that mediate activation of the enzyme in response to diacylglycerol (DAG) or phorbol ester (2,3). In addition to lipid-mediated activation, PKD catalytic activity can also be stimulated via phosphorylation of critical serine residues within the activation loop of the enzyme (4-8). Novel PKCs, such as PKCη and PKCε, have been shown to phosphorylate PKD1 at Ser744 and Ser748 (Ser706 and Ser710 in human PKD2), resulting in alleviation of autoinhibition of the enzyme mediated by PH domain interactions with the catalytic domain (5). Phosphorylation and activation of PKD isoforms has also been described for other upstream kinases. For example, casein kinase 2 (CK2) has been shown to phosphorylate PKD2 at Ser244, which promotes nuclear accumulation of PKD2, phosphorylation of HDAC7, and expression of Nur77 (9). Although only a handfull of PKD2 effectors have been identified, PKD2 has been implicated in regulating an array of cellular events, including cell survival, development, growth, migration, and transformation (10-14). PKD2-mediated phosphorylation of at least one known substrate, phosphatidylinositol 4-kinase type IIIβ (PI4KIIIβ), also implicates PKD2 in the formation and regulation of exocytotic transport vesicles from the trans Golgi network (15).

  1. Rykx, A. et al. (2003) FEBS Lett 546, 81-6.
  2. Sturany, S. et al. (2001) J Biol Chem 276, 3310-8.
  3. Chen, J. et al. (2008) Biochem J 411, 333-42.
  4. Zugaza, J.L. et al. (1996) EMBO J 15, 6220-30.
  5. Waldron, R.T. et al. (2001) J Biol Chem 276, 32606-15.
  6. Waldron, R.T. and Rozengurt, E. (2003) J Biol Chem 278, 154-63.
  7. Sinnett-Smith, J. et al. (2009) J Biol Chem 284, 13434-45.
  8. Konopatskaya, O. et al. (2011) Blood, Epub ahead of print.
  9. von Blume, J. et al. (2007) EMBO J 26, 4619-33.
  10. Mihailovic, T. et al. (2004) Cancer Res 64, 8939-44.
  11. Irie, A. et al. (2006) Int Immunol 18, 1737-47.
  12. Sinnett-Smith, J. et al. (2007) J Cell Physiol 211, 781-90.
  13. Hao, Q. et al. (2009) J Biol Chem 284, 799-806.
  14. Kleger, A. et al. (2011) PLoS One 6, e14599.
  15. Pusapati, G.V. et al. (2010) Mol Biol Cell 21, 1011-22.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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