Histone Methyltransferase Set7/9, Recombinant, Human

Set 7/9 is a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine(AdoMet). The methylation of lysine residues of histones plays a critical role in the regulation of chromatin structure and gene expression. Acetylation, phosphorylation and methylation of the amino-terminal tails of histone are thought to be involved in the regulation of chromatin structure and function. The enzymes identified in the methylation of specific lysine residue on histones belong to the SET family with just one exception. Set7/9, unlike most other SET proteins, is exclusively a mono-methylase. Recombinant Human HMTase produced in E.Coli is a single,non-glycosylated polypeptide chain containing 366 amino acids & having a molecular mass of 40.7kD.\n\nSequence: \nMDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP\n\nStability: \nStore at 4 degrees C if entire vial will be used within 1-2 weeks. Store, frozen at -20 degrees C for longer periods of time. Please avoid freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

H5203-97

Size

20ug

Form

Supplied as a liquid in 50mM Tris-HCl, pH 7.5, 0.2M sodium chloride, 5mM DTT and 20% glycerol.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures.\n\nJ Am Chem Soc 2006 Feb 1;128(4):1272-8\n\n2. Structural basis for the methylation site specificity of SET7/9.\n\nNat Struct Mol Biol 2006 Feb;13(2):140-6\n\n3. Structure and catalytic mechanism of the human histone methyltransferase SET7/9.\n\nNature 2003 Feb 6;421(6923):652-6\n\n4. Crystal structure and functional analysis of the histone methyltransferase SET7/9.\n\nCell 2002 Oct 4;111(1):105-15