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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-PKD/PKCμ (Ser916) Antibody 2051 1 x 40 µl
H M R Mk 115 Rabbit 
PKD/PKCμ Antibody 2052 1 x 40 µl
H M R Mk 115 Rabbit 
Phospho-PKD/PKCμ (Ser744/748) Antibody 2054 1 x 40 µl
H M R Mk 115 Rabbit 
Phospho-PKC (pan) (βII Ser660) Antibody 9371 1 x 40 µl
H M R Mk 78, 80, 82, 85 Rabbit 
Phospho-PKCα/β II (Thr638/641) Antibody 9375 1 x 40 µl
H M Mk 80, 82 Rabbit 
Phospho-PKCδ (Thr505) Antibody 9374 1 x 40 µl
H M 78 Rabbit 
Phospho-PKCδ/θ (Ser643/676) Antibody 9376 1 x 40 µl
H M R Mk X 78 Rabbit 
Phospho-PKCθ (Thr538) Antibody 9377 1 x 40 µl
H R Mk B 79 Rabbit 
Phospho-PKCζ/λ (Thr410/403) Antibody 9378 1 x 40 µl
H M R Mk 76 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 1 x 100 µl
All Goat 

Product Description

The Phospho-PKC Antibody Sampler Kit provides a fast and economical means of evaluating multiple PKC isoforms and their phosphorylation state. The kit contains enough primary and secondary antibodies to perform four Western blot experiments.


Specificity / Sensitivity

Phospho-PKC (pan) (βII Ser660) Antibody detects PKCα, β I, β II, δ, ε and η isoforms only when phosphorylated at a carboxy-terminal residue homologous to Ser660 of PKCβ II. Phospho-PKCδ (Ser643) Antibody detects PKC δ when phosphorylated at Ser643, and PKCθ when phosphorylated at Ser676. PKD/PKCμ antibody detects PKD/PKCμ only. All other phospho-PKC antibodies recognize only their specific isoform when phosphorylated at the indicated sites.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to the sequence of the human protein PKCβ II, PKCα, PKCδ, PKCθ, PKCζ or the mouse protein (PKD). Antibodies are purified by protein A and peptide affinity chromatography.

Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).


1.  Nishizuka, Y. (1984) Nature 308, 693-8.

2.  Keranen, L.M. et al. (1995) Curr Biol 5, 1394-1403.

3.  Mellor, H. and Parker, P.J. (1998) Biochem J 332 ( Pt 2), 281-92.

4.  Ron, D. and Kazanietz, M.G. (1999) FASEB J 13, 1658-76.

5.  Moscat, J. and Diaz-Meco, M.T. (2000) EMBO Rep 1, 399-403.

6.  Baron, C.L. and Malhotra, V. (2002) Science 295, 325-8.

7.  Flynn, P. et al. (2000) J Biol Chem 275, 11064-70.


Entrez-Gene Id 5578, 5579, 5580, 5581, 5583, 5582, 5584, 5588, 5590, 5587
Swiss-Prot Acc. P17252, P05771, P05771-2, Q05655, Q02156, P24723, P05129, P41743, Q04759, Q05513, Q15139

Protein Specific References

Abdala-Valencia H and Cook-Mills JM (2006) J Immunol 177, 6379–87

Abdala-Valencia H and Cook-Mills JM (2006) J Immunol 177, 6379–87

Leinweber B et al. (2000) J Biol Chem 275, 40329–36

Zhu M et al. (2013) Cardiovasc Diabetol 12, 13

Leinweber B et al. (2000) J Biol Chem 275, 40329–36

Zhu M et al. (2013) Cardiovasc Diabetol 12, 13

Zrachia A et al. (2002) J Biol Chem 277, 23693–701

Zhang L et al. (2004) J Biol Chem 279, 28315–9

Balasubramanian S et al. (2006) J Biol Chem 281, 36162–72

Liu Y et al. (2006) J Biol Chem 281, 12102–11

Welman A et al. (2007) Protein Sci 16, 2711–5

Lu W et al. (2007) Cell Signal 19, 2165–73

Basu A et al. (2009) Cell Signal 21, 1680–5

Zrachia A et al. (2002) J Biol Chem 277, 23693–701

Zhang L et al. (2004) J Biol Chem 279, 28315–9

Balasubramanian S et al. (2006) J Biol Chem 281, 36162–72

Liu Y et al. (2006) J Biol Chem 281, 12102–11

Welman A et al. (2007) Protein Sci 16, 2711–5

Lu W et al. (2007) Cell Signal 19, 2165–73

Basu A et al. (2009) Cell Signal 21, 1680–5

Zrachia A et al. (2002) J Biol Chem 277, 23693–701

Zhang L et al. (2004) J Biol Chem 279, 28315–9

Balasubramanian S et al. (2006) J Biol Chem 281, 36162–72

Liu Y et al. (2006) J Biol Chem 281, 12102–11

Welman A et al. (2007) Protein Sci 16, 2711–5

Lu W et al. (2007) Cell Signal 19, 2165–73

Basu A et al. (2009) Cell Signal 21, 1680–5

Cenni V et al. (2002) Biochem J 363, 537–45

Faisal A et al. (2008) J Biol Chem 283, 18591–600

Rose AJ et al. (2004) J Physiol 561, 861–70

Freeley M et al. (2005) Biochem Biophys Res Commun 334, 619–30

Freeley M et al. (2005) Biochem Biophys Res Commun 334, 619–30

Freeley M et al. (2005) Biochem Biophys Res Commun 334, 619–30

Smith L et al. (2003) Biochem J 375, 663–71

Guha S et al. (2002) Cancer Res 62, 1632–40

Kennett SB et al. (2004) J Biol Chem 279, 3300–7

Phan D et al. (2011) Biochem Biophys Res Commun 411, 335–41

Guha S et al. (2002) Cancer Res 62, 1632–40

Kennett SB et al. (2004) J Biol Chem 279, 3300–7

Phan D et al. (2011) Biochem Biophys Res Commun 411, 335–41

Guha S et al. (2002) Cancer Res 62, 1632–40

Kennett SB et al. (2004) J Biol Chem 279, 3300–7

Phan D et al. (2011) Biochem Biophys Res Commun 411, 335–41


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