Rabbit anti Human SET Phosphatase 2A Inhibitor I2PP2A
| Code | Size | Price |
|---|
| EXA-X2332P | 100 ug | £316.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Rabbit
Antibody Isotype: IgG
Antibody Clonality: Polyclonal
Regulatory Status: RUO
Target Species: Human
Application: Western Blot (WB)
Shipping:
Ship on gel ice store at -20°C immediately upon arrival
Storage:
Product should be stored at -70°C. Aliquot to avoid freeze/thaw cycles
Further Information
Applications Description:
Antibody can be used for Western blotting (1:400 dilution). Optimal concentration should be evaluated by serial dilutions.
Background:
Human SET was originally identified as part of the SET-CAN fusion gene produced by a somatic translocation event in a patient with acute undifferentiated leukemia. In developing kidney, SET is highly expressed in the zone of nephron morphogenesis. SET has been shown to be a potent and specific inhibitor of protein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cell proliferation and differentiation. SET is also involved in the regulation of renal cell proliferation and tumorigenesis. SET mRNA expression is markedly reduced in cells rendered quiescent by serum starvation, contact inhibition, or differentiation. SET protein expression is also much greater in developing rat and human kidney than in fully differentiated, mature kidney. High levels of SET mRNA and SET protein expression arefound in Wilms' tumor, but not in renal cell carcinoma, adult polycystic kidney disease or in transitional cell carcinoma.
Caution:
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
Concentration:
Lot specific, see vial
Field of Interest:
Lipid Mediators
Formulation:
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Functional Analysis:
Western Blotting
Immunogen:
Synthetic peptide derived from the human SET protein
Positive Control:
Widely expressed. Low levels in quiescent cells during serum starvation, contact inhibition or differentiation. Highly expressed in Wilms' tumor.
Product Form:
Affinity Purified
Product Stability:
Products are stable for one year from purchase when stored properly
Purification Method:
Antigen Immunoaffiinity Purification
Synonyms:
SET, SET translocation (myeloid leukemia-associated), Protein SET, Phosphatase 2A inhibitor, I2PP2A, I-2PP2A, Template-activating factor I, TAF-I, HLA-DR-associated protein II, PHAPII, Inhibitor of granzyme A-activated DNase, IGAAD2PP2A; IGAAD; I2PP2A;
UniProt:
Q01105
References
[1] von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G.;
Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.; Mol. Cell. Biol. 12:3346-3355(1992).
[2] von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G.;
Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.; Mol. Cell. Biol. 12:3346-3355(1992).
[3] Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.; Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII.; Biol. Chem. Hoppe-Seyler 375:113-126(1994).
[4] Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., Okuda A., Kikuchi A., Matsumoto K.; Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.; Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995).
[5] Li M., Makkinje A., Damuni Z.; The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A.; J. Biol. Chem. 271:11059-11062(1996).
[6] Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.; Inhibitors of protein phosphatase-2A from human brain: structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated Tau.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[7] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).; Genome Res. 14:2121-2127(2004).
[8] Adachi Y., Pavlaki G.N., Copeland T.D.; Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia.; J. Biol. Chem. 269:2258-2262(1994).
[9] Wang L.C., Chen Y.; A relative factor in human rectum carcinoma.; Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[10] Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D., Ballermann B.J.;
Expression of SET, an inhibitor of protein phosphatase 2A, in renal development and Wilms' tumor.; J. Am. Soc. Nephrol. 9:1873-1880(1998).
[11] Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.;
Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein.; Cell 104:119-130(2001).
[12] Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K., Adachi Y.; Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET.; Eur. J. Biochem. 268:1340-1351(2001).
[13] Fan Z., Beresford P.J., Zhang D., Lieberman J.; HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A.; Mol. Cell. Biol. 22:2810-2820(2002).
[14] Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.; Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor.; Cell 112:659-672(2003).
[15] Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.; Cell 115:241-241(2003).
[16] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.;
Cell 127:635-648(2006).
[17] Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.; Mol. Cell 23:607-618(2006).
[18] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.; Mol. Cell. Biol. 12:3346-3355(1992).
[2] von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G.;
Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.; Mol. Cell. Biol. 12:3346-3355(1992).
[3] Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.; Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII.; Biol. Chem. Hoppe-Seyler 375:113-126(1994).
[4] Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., Okuda A., Kikuchi A., Matsumoto K.; Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.; Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995).
[5] Li M., Makkinje A., Damuni Z.; The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A.; J. Biol. Chem. 271:11059-11062(1996).
[6] Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.; Inhibitors of protein phosphatase-2A from human brain: structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated Tau.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[7] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).; Genome Res. 14:2121-2127(2004).
[8] Adachi Y., Pavlaki G.N., Copeland T.D.; Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia.; J. Biol. Chem. 269:2258-2262(1994).
[9] Wang L.C., Chen Y.; A relative factor in human rectum carcinoma.; Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[10] Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D., Ballermann B.J.;
Expression of SET, an inhibitor of protein phosphatase 2A, in renal development and Wilms' tumor.; J. Am. Soc. Nephrol. 9:1873-1880(1998).
[11] Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.;
Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein.; Cell 104:119-130(2001).
[12] Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K., Adachi Y.; Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET.; Eur. J. Biochem. 268:1340-1351(2001).
[13] Fan Z., Beresford P.J., Zhang D., Lieberman J.; HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A.; Mol. Cell. Biol. 22:2810-2820(2002).
[14] Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.; Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor.; Cell 112:659-672(2003).
[15] Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.; Cell 115:241-241(2003).
[16] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.;
Cell 127:635-648(2006).
[17] Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.; Mol. Cell 23:607-618(2006).
[18] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).