ABIN4620361
antibody from antibodies-online
Targeting: SET
2PP2A, IGAAD, IPP2A2, PHAPII, TAF-I, TAF-IBETA
Antibody data
- Antibody Data
- Antigen structure
- References [12]
- Comments [0]
- Validations [0]
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- Product number
- ABIN4620361 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-SET Nuclear Oncogene (SET) antibody
- Antibody type
- Polyclonal
- Description
- Affinity chromatography
- Reactivity
- Human
- Host
- Rabbit
- Isotype
- IgG
- Vial size
- 0.1 mg
- Storage
- Store the product (in aliquots) at -20°C to -70°C. Can be shipped at 2 - 8°C.
- Handling
- Avoid repeated freezing and thawing.
Submitted references Particle size distributions and health-related exposures of polychlorinated dibenzo-p-dioxins and dibenzofurans (PCDD/Fs) of sinter plant workers.
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau.
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor.
Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET.
Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein.
Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A.
Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.
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.
Shih TS, Shih M, Lee WJ, Huang SL, Wang LC, Chen YC, Tsai PJ
Chemosphere 2009 Mar;74(11):1463-70
Chemosphere 2009 Mar;74(11):1463-70
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.
Molina H, Horn DM, Tang N, Mathivanan S, Pandey A
Proceedings of the National Academy of Sciences of the United States of America 2007 Feb 13;104(7):2199-204
Proceedings of the National Academy of Sciences of the United States of America 2007 Feb 13;104(7):2199-204
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M
Cell 2006 Nov 3;127(3):635-48
Cell 2006 Nov 3;127(3):635-48
Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y
Molecular cell 2006 Aug;23(4):607-18
Molecular cell 2006 Aug;23(4):607-18
Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau.
Tsujio I, Zaidi T, Xu J, Kotula L, Grundke-Iqbal I, Iqbal K
FEBS letters 2005 Jan 17;579(2):363-72
FEBS letters 2005 Jan 17;579(2):363-72
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J, MGC Project Team.
Genome research 2004 Oct;14(10B):2121-7
Genome research 2004 Oct;14(10B):2121-7
Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor.
Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J
Cell 2003 Mar 7;112(5):659-72
Cell 2003 Mar 7;112(5):659-72
Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET.
Minakuchi M, Kakazu N, Gorrin-Rivas MJ, Abe T, Copeland TD, Ueda K, Adachi Y
European journal of biochemistry 2001 Mar;268(5):1340-51
European journal of biochemistry 2001 Mar;268(5):1340-51
Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein.
Seo SB, McNamara P, Heo S, Turner A, Lane WS, Chakravarti D
Cell 2001 Jan 12;104(1):119-30
Cell 2001 Jan 12;104(1):119-30
Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A.
Li M, Makkinje A, Damuni Z
Biochemistry 1996 Jun 4;35(22):6998-7002
Biochemistry 1996 Jun 4;35(22):6998-7002
Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.
Nagata K, Kawase H, Handa H, Yano K, Yamasaki M, Ishimi Y, Okuda A, Kikuchi A, Matsumoto K
Proceedings of the National Academy of Sciences of the United States of America 1995 May 9;92(10):4279-83
Proceedings of the National Academy of Sciences of the United States of America 1995 May 9;92(10):4279-83
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.
von Lindern M, van Baal S, Wiegant J, Raap A, Hagemeijer A, Grosveld G
Molecular and cellular biology 1992 Aug;12(8):3346-55
Molecular and cellular biology 1992 Aug;12(8):3346-55
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