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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-Stat1 (Tyr701) (D4A7) Rabbit mAb 7649 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M R 84, 91 Rabbit IgG
Phospho-Stat2 (Tyr690) Antibody 4441 40 µl
Western Blotting
H 113 Rabbit 
Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb 9145 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M R Mk 79, 86 Rabbit IgG
Phospho-Stat3 (Ser727) Antibody 9134 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Chromatin Immunoprecipitation
H M R 86 Rabbit 
Phospho-Stat5 (Tyr694) (D47E7) XP® Rabbit mAb 4322 40 µl
Western Blotting Immunofluorescence Flow Cytometry
H M 90 Rabbit IgG
Phospho-Stat6 (Tyr641) Antibody 9361 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Flow Cytometry
H 110 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Phospho-Stat Pathway Sampler Kit provides an economical means to evaluate the activation status of Stat molecules, including the phosphorylation of Stat1 at Tyr701, Stat2 at Tyr690, Stat3 at Tyr705/Ser727, Stat5 at Tyr694 and Stat6 at Tyr641. The kit includes enough primary and secondary antibody to perform four Western blot experiments.


Specificity / Sensitivity

Each phospho-Stat antibody in the kit recognizes only the phosphorylated form of its specific target.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptides corresponding to residues surrounding Tyr690 of human Stat2, Ser727 of mouse Stat3, or Tyr641 of human Stat6. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr701 of human Stat1 protein, Tyr705 of mouse Stat3, or residues surrounding Tyr694 of human Stat5a protein.

Jaks (Janus Kinases) and Stats (Signal Transducers and Activators of Transcription) are utilized by receptors for a wide variety of ligands including cytokines, hormones, growth factors and neurotransmitters. Jaks, activated via autophosphorylation following ligand-induced receptor aggregation, phosphorylate tyrosine residues on associated receptors, Stat molecules and other downstream signaling proteins (1,2). The phosphorylation of Stat proteins at conserved tyrosine residues activates SH2-mediated dimerization followed rapidly by nuclear translocation. Stat dimers bind to IRE (interferon response element) and GAS (gamma interferon-activated sequence) DNA elements, resulting in the transcriptional regulation of downstream genes (1,2). The remarkable range and specificity of responses regulated by the Stats is determined in part by the tissue-specific expression of different cytokine receptors, Jaks and Stats (2,3), and by the combinatorial coupling of various Stat members to different receptors. Serine phosphorylation in the carboxy-terminal transcriptional activation domain has been shown to regulate the function of Stat1, -2, -3, -4 and -5 (1). Phosphorylation of Stat3 at Ser727 via MAPK or mTOR pathways is required for optimal transcriptional activation in response to growth factors and cytokines including IFN-gamma and CNTF (4,5). Jak/Stat pathways also play important roles in oncogenesis, tumor progression, angiogenesis, cell motility, immune responses and stem cell differentiation (6-11).


1.  Leonard, W.J. (1998) Annu. Rev. Immunol. 16, 293-322.

2.  Caldenhoven, E. et al. (1996) J Biol Chem 271, 13221-7.

3.  Bromberg, J.F. et al. (1999) Cell 98, 295-303.

4.  Dentelli, P. et al. (1999) J Immunol 163, 2151-9.

5.  Darnell, J.E. et al. (1994) Science 264, 1415-21.

6.  Lim, C.P. and Cao, X. (1999) J. Biol. Chem. 274, 31055-31061.

7.  Wen, Z. et al. (1995) Cell 82, 241-50.

8.  Su, L. et al. (1999) J. Biol. Chem. 274, 31770-31774.

9.  Yokogami, K. et al. (2000) Curr Biol 10, 47-50.

10.  Cattaneo, E. et al. (1999) Trends Neurosci. 22, 365-369.

11.  Frank, D.A. (1999) Mol. Med. 5, 432-456.


Entrez-Gene Id 6772, 6773, 6774, 6776, 6777, 6778
Swiss-Prot Acc. P42224, P52630, P40763, P42229, P51692, P42226

Product Specific References

Lee, J. et al. (2011) Oncogene , .

Protein Specific References

Dimberg A et al. (2000) Blood 96, 2870–8

Mowen KA et al. (2001) Cell 104, 731–41

Zhu W et al. (2002) J Biol Chem 277, 35787–90

Chen Q et al. (2002) Immunology 107, 199–208

Nair JS et al. (2002) Proc Natl Acad Sci U S A 99, 5971–6

DeVries TA et al. (2004) J Biol Chem 279, 45603–12

Timofeeva OA et al. (2006) Oncogene 25, 7555–64

Liu X et al. (2008) J Immunol 181, 449–63

Vanhatupa S et al. (2008) Biochem J 409, 179–85

Roth A et al. (2010) Proc Natl Acad Sci U S A 107, 19502–7

Chen Z et al. (2011) Cell Signal 23, 1404–12

Antunes F et al. (2011) Mol Cell Biol 31, 3029–37

Grönholm J et al. (2012) BMC Biochem 13, 20

Ng J and Cantrell D (1997) J Biol Chem 272, 24542–9

Schuringa JJ et al. (2000) Blood 95, 3765–70

Duarte RF and Frank DA (2000) Blood 96, 3422–30

Schuringa JJ et al. (2001) Oncogene 20, 5350–8

Deb A et al. (2001) EMBO J 20, 2487–96

Abe K et al. (2001) Oncogene 20, 3464–74

Kopantzev Y et al. (2002) Oncogene 21, 6791–800

Sun S and Steinberg BM (2002) J Gen Virol 83, 1651–8

Hwang JH et al. (2003) Mol Endocrinol 17, 1155–66

Lo RK et al. (2003) J Biol Chem 278, 52154–65

Liu H et al. (2003) Blood 102, 344–52

Lo RK and Wong YH (2004) Mol Pharmacol 65, 1427–39

Wang R et al. (2005) J Biol Chem 280, 11528–34

Yuan ZL et al. (2005) Science 307, 269–73

Ray S et al. (2005) Gastroenterology 129, 1616–32

Liu AM et al. (2006) J Biol Chem 281, 35812–25

Zhang X et al. (2007) Proc Natl Acad Sci U S A 104, 4060–4

Ohbayashi N et al. (2007) Biol Pharm Bull 30, 1860–4

Nadiminty N et al. (2007) Biochem Biophys Res Commun 359, 379–84

Duechting A et al. (2008) J Virol 82, 7942–52

Chen CL et al. (2008) Mol Cancer 7, 78

Hatziapostolou M et al. (2011) Cell 147, 1233–47

Sestito R et al. (2011) FASEB J 25, 916–27

Gupta M et al. (2012) Leukemia 26, 1356–64

Ng J and Cantrell D (1997) J Biol Chem 272, 24542–9

Schuringa JJ et al. (2000) Blood 95, 3765–70

Duarte RF and Frank DA (2000) Blood 96, 3422–30

Schuringa JJ et al. (2001) Oncogene 20, 5350–8

Deb A et al. (2001) EMBO J 20, 2487–96

Abe K et al. (2001) Oncogene 20, 3464–74

Kopantzev Y et al. (2002) Oncogene 21, 6791–800

Sun S and Steinberg BM (2002) J Gen Virol 83, 1651–8

Hwang JH et al. (2003) Mol Endocrinol 17, 1155–66

Lo RK et al. (2003) J Biol Chem 278, 52154–65

Liu H et al. (2003) Blood 102, 344–52

Lo RK and Wong YH (2004) Mol Pharmacol 65, 1427–39

Wang R et al. (2005) J Biol Chem 280, 11528–34

Yuan ZL et al. (2005) Science 307, 269–73

Ray S et al. (2005) Gastroenterology 129, 1616–32

Liu AM et al. (2006) J Biol Chem 281, 35812–25

Zhang X et al. (2007) Proc Natl Acad Sci U S A 104, 4060–4

Ohbayashi N et al. (2007) Biol Pharm Bull 30, 1860–4

Nadiminty N et al. (2007) Biochem Biophys Res Commun 359, 379–84

Duechting A et al. (2008) J Virol 82, 7942–52

Chen CL et al. (2008) Mol Cancer 7, 78

Hatziapostolou M et al. (2011) Cell 147, 1233–47

Sestito R et al. (2011) FASEB J 25, 916–27

Gupta M et al. (2012) Leukemia 26, 1356–64

Fox EM et al. (2008) Mol Endocrinol 22, 1781–96

Chen H et al. (2011) Cell 147, 436–46

Shirakawa T et al. (2011) J Biol Chem 286, 4003–10


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