Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN2845290 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-SET Domain Containing 8 Pseudogene 1 (SETD8P1) (AA 289-317), (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- AA 289-317, C-Term
- Antibody clone number
- RB5744
- Vial size
- 80 μL
- Storage
- Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
Submitted references Regulation of p53 activity through lysine methylation.
Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.
Structure and catalytic mechanism of the human histone methyltransferase SET7/9.
Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.
Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D
Nature 2004 Nov 18;432(7015):353-60
Nature 2004 Nov 18;432(7015):353-60
Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.
Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y
The EMBO journal 2003 Jan 15;22(2):292-303
The EMBO journal 2003 Jan 15;22(2):292-303
Structure and catalytic mechanism of the human histone methyltransferase SET7/9.
Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ
Nature 2003 Feb 6;421(6923):652-6
Nature 2003 Feb 6;421(6923):652-6
Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W
Genes & development 2003 Apr 1;17(7):896-911
Genes & development 2003 Apr 1;17(7):896-911
Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.
Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D
Genes & development 2002 Feb 15;16(4):479-89
Genes & development 2002 Feb 15;16(4):479-89
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