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SET7/9 (human), (recombinant)

 
ALX-201-178-C100 100 µg 286.00 USD
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Product Specification

Alternative Name:Histone H3-K4 methyltransferase
 
MW:~40.7kDa.
 
Source:Produced in E. coli.
 
EC:2.1.1.43
 
UniProt ID:Q8WTS6
 
Concentration:1mg/ml
 
Formulation:Liquid. In 50mM TRIS-HCl, pH 7.5, containing 0.2M sodium chloride, 5mM DTT and 20% glycerol.
 
Purity:≥95% (SDS-PAGE)
 
Endotoxin Content:<1.0EU/µg protein (LAL test)
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Handling:Avoid freeze/thaw cycles.
 
Scientific Background:Histone methyltransferase that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine.
 
SET7/9 (human), (recombinant) SDS-PAGE
10% SDS-PAGE of human SET7/9 (Prod. No. ALX-201-178).
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SET7/9 (human), (recombinant) SDS-PAGE

Product Literature References

Identification and Characterizations of Novel, Selective Histone Methyltransferase SET7 Inhibitors by Scaffold Hopping- and 2D-Molecular Fingerprint-Based Similarity Search: H. Ding, et al.; Molecules 23, E567 (2018), Abstract; Full Text
Miniaturization of High-Throughput Epigenetic Methyltransferase Assays with Acoustic Liquid Handling: B. Edwards, et al.; J. Lab. Autom. 21, 208 (2016), Abstract;
Modulations of DNA Contacts by Linker Histones and Post-translational Modifications Determine the Mobility and Modifiability of Nucleosomal H3 Tails: A. Stutzer, et al.; Mol. Cell 61, 247 (2016), Abstract;
Development of homogeneous nonradioactive methyltransferase and demethylase assays targeting histone H3 lysine 4: N. Gauthier, et al.; J. Biomol. Screen. 17, 49 (2012), Abstract;
Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production: K. Bonham, et al.; FEBS J. 277, 2096 (2010), Abstract; Full Text
Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet: T. Kwon, et al.; EMBO J. 22, 292 (2003), Abstract;

General Literature References

Structure and catalytic mechanism of the human histone methyltransferase SET7/9: B. Xiao, et al.; Nature 421, 652 (2003), Abstract;

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