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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-PTEN (Ser380/Thr382/383) (44A7) Rabbit mAb 9549 40 µl
Western Blotting
H M R Mk 54 Rabbit IgG
PTEN (D4.3) XP® Rabbit mAb 9188 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry
H M R Mk Dg 54 Rabbit IgG
Phospho-PDK1 (Ser241) (C49H2) Rabbit mAb 3438 40 µl
Western Blotting Immunoprecipitation
H M R 58 to 68 Rabbit IgG
PDK1 Antibody 3062 40 µl
Western Blotting
H M R Mk 58 to 68 Rabbit 
Non-phospho PTEN (Ser380/Thr382/Thr383) (D2D11) Rabbit mAb 7960 40 µl
Western Blotting Immunoprecipitation
H M R Mk 55 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The PTEN and PDK1 Sampler Kit provides an economical means to evaluate two key enzymes that regulate multiple signaling pathways. The kit contains enough primary and secondary antibodies to perform four Western blots per primary antibody.


Specificity / Sensitivity

Each antibody in the PTEN and PDK1 Antibody Sampler Kit detects endogenous levels of its target protein. Activation state antibodies detect only target proteins phosphorylated at indicated residues. Non-Phospho-PTEN (Ser380/Thr382/Thr383) Antibody detects endogenous levels of PTEN only when dephosphorylated at Ser380, Thr382 and Thr383.


Source / Purification

Phospho-specific rabbit monoclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues around Ser380, Thr382 and Thr383 of human PTEN and around Ser241 of human PDK1. PTEN (D4.3) XP® Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues in the carboxy-terminal sequence of human PTEN. Monoclonal antibody Non-phospho PTEN (Ser380/Thr382/Thr383) (D2D11) is produced by immunizing animals with a synthetic non-phosphopeptide corresponding to residues surrounding Ser380/Thr382/Thr383 of human PTEN protein. Polyclonal PDK1 antibody is produced by immunizing animals with synthetic peptides corresponding to residues surrounding the carboxy terminus of human PDK1. Polyclonal antibodies are purified using protein A and peptide affinity chromatography.

PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).


Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (11,12) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (13). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.


1.  Wan X and Helman LJ (2003) Oncogene 22, 8205–11

2.  Myers, M.P. et al. (1997) Proc Natl Acad Sci USA 94, 9052-7.

3.  Myers, M.P. et al. (1998) Proc Natl Acad Sci USA 95, 13513-8.

4.  Wu, X. et al. (1998) Proc Natl Acad Sci USA 95, 15587-91.

5.  Vazquez, F. et al. (2000) Mol Cell Biol 20, 5010-8.

6.  Torres, J. and Pulido, R. (2001) J Biol Chem 276, 993-8.

7.  Freeman, D.J. et al. (2003) Cancer Cell 3, 117-30.

8.  Funamoto, S. et al. (2002) Cell 109, 611-23.

9.  Cantley, L.C. and Neel, B.G. (1999) Proc Natl Acad Sci USA 96, 4240-5.

10.  Iijima, M. and Devreotes, P. (2002) Cell 109, 599-610.

11.  Belham, C. et al. (1999) Curr. Biol. 9, R93-R96.

12.  Toker, A. and Newton, A.C. (2000) Cell 103, 185-188.

13.  Williams, M.R. et al. (2000) Curr. Biol. 10, 439-448.


Entrez-Gene Id 5170, 5728
Swiss-Prot Acc. O15530, P60484

Protein Specific References

Sato S et al. (2002) J Biol Chem 277, 39360–7

Kim DW et al. (2003) Mol Endocrinol 17, 1382–94

Fiory F et al. (2005) Mol Cell Biol 25, 10803–14

Al-Khouri AM et al. (2005) J Biol Chem 280, 35195–202

Okumura K et al. (2006) J Biol Chem 281, 26562–8

Ikenoue T et al. (2008) Cancer Res 68, 6908–12

Maddika S et al. (2011) Nat Cell Biol 13, 728–33

Zhang XC et al. (2012) Biochem J 444, 457–64

González-Santamaría J et al. (2012) Cell Death Dis 3, e393

Putz U et al. (2012) Sci Signal 5, ra70

Bassi C et al. (2013) Science 341, 395–9

Kavela, S. et al. (2013) Cancer Res 73, 205-14.

Al-Khouri AM et al. (2005) J Biol Chem 280, 35195–202

Okumura K et al. (2006) J Biol Chem 281, 26562–8

Ikenoue T et al. (2008) Cancer Res 68, 6908–12

Maddika S et al. (2011) Nat Cell Biol 13, 728–33

Zhang XC et al. (2012) Biochem J 444, 457–64

González-Santamaría J et al. (2012) Cell Death Dis 3, e393

Putz U et al. (2012) Sci Signal 5, ra70

Bassi C et al. (2013) Science 341, 395–9

Kavela, S. et al. (2013) Cancer Res 73, 205-14.

Al-Khouri AM et al. (2005) J Biol Chem 280, 35195–202

Okumura K et al. (2006) J Biol Chem 281, 26562–8

Ikenoue T et al. (2008) Cancer Res 68, 6908–12

Maddika S et al. (2011) Nat Cell Biol 13, 728–33

Zhang XC et al. (2012) Biochem J 444, 457–64

González-Santamaría J et al. (2012) Cell Death Dis 3, e393

Putz U et al. (2012) Sci Signal 5, ra70

Bassi C et al. (2013) Science 341, 395–9

Kavela, S. et al. (2013) Cancer Res 73, 205-14.


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U.S. Patent No. 5,675,063.