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Human SETD7 / SET7/9 Protein (His Tag)

KMT7,SET7,SET7/9,SET9

Catalog Number P11209-H07E
Organism Species Human
Host E. coli
Synonyms KMT7,SET7,SET7/9,SET9
Molecular Weight The recombinant human SETD7 comprises 372 amino acids and has a predicted molecular mass of 41.5 kDa. It migrates as an approximately 48 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 94 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human SETD7 (NP_085151.1) (Asp 2-Lys 366) was expressed, with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Epigenetics |Histone Modifying Enzymes |Methylation and Demethylation |Histone methylation
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Histone-lysine N-methyltransferase SETD7, also known as SET domain containing (lysine methyltransferase) 7, SET7/9, Histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, and SETD7, is a member of the histone-lysine methyltransferase family and SET7 subfamily. SETD7 is widely expressed and expressed in pancreatic islets. SETD7 contains three MORN repeats and one SET domain. SETD7 plays a central role in the transcriptional activation of genes such as collagenase or insulin. As a protein lysine methyltransferase (PKMT), SETD7 also has methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding in substrate proteins. The mono-methyltransferase activity of SETD7 is achieved by disrupting the formation at near-attack conformations for the dimethylation reaction. SETD7 is also a novel coactivator of NF-kappaB and plays a role in inflammation and diabetes.
Reference
  • Wang, H. et al., 2002, Mol Cell 8 (6): 1207-17. 
  • Jacobs, SA. et al., 2002, Nat. Struct. Biol. 9 (11): 833-8. 
  • Xiao B, et al., 2003, Nature. 421 (6923): 652-6.
  • Martens, JH. et al., 2003, Mol. Cell. Biol. 23: 1808-1816.
  • Couture, JF. et al., 2006, Nat Struct Mol Biol  13 (2): 140-6.