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SMYD3, Recombinant Human

Cat. No.: 15-1007
List Price: $219.00

Product Description

Type:  HMT Host:  E. coli
Mol Wgt.:  68 kDa Epitope Tag:  GST

Recombinant SMYD3 Enzyme Description: Recombinant full-length human SMYD3 protein, (SET and MYND domain-containing protein 3, ZMYND1, ZNFN3A1, accession Q9H7B4), containing an N-terminal GST tag, expressed in E. coli. SMYD3 is a protein lysine methyltransferase that has been shown to catalyze mono-, di-, and tri-methylation of histone H4 at lysine 5 by multiple independent approaches, including mass spectrometry. SMYD3 levels are up-regulated in a large number of tumors, including liver, breast and rectal carcinomas. SMYD3 overexpression promotes the proliferation of cancer cells, while its depletion slows expansion.

Recombinant SMYD3 Enzyme Formulation: Recombinant GST-SMYD3 (1 µg/µl) in 100mM Tris pH 8.0, 10 mM glutathione and 10% glycerol.

Storage and Stability: Stable for six months at -80°C from date of receipt. For best results, aliquot and avoid multiple freeze/thaws.

Application Notes: Recombinant SMYD3, human is useful for histone H4 methylation experiments, enzyme kinetics and inhibitor screening. Use of 1-3 µg SMYD3 per reaction with recombinant histone H4 as a substrate is recommended.

Van Aller GS et al (2012). Epigenetics 7: 340-343. Link
Mazur PK et al (2014). Nature 510: 283-287. Link
Peserico A et al (2015). J Cell Pysiol DOI 10.1002/jcp.24975. Link

View technical datasheet for this product. 15-1007 Datasheet
15-1007 Gel and Enzyme Activity Data

Enzyme Activity Data: Recombinant SMYD3, human (1 µg) was used in a methylation assay with 1 µg recombinant human histone H4 and radioactive SAM and the reaction was run on a PAGE gel. Lane 1: GST only vector. Lane 2: GST-SMYD3 vector. Left Panel: Coomassie stained gel. Right panel: Autoradiograph.
(Click image to enlarge)

15-1007 Protein Gel Data

Protein Gel Data: Recombinant human SMYD3 (1 µg) run on a PAGE gel and stained with Coomassie blue. Migration and molecular weight of protein standards is indicated.
(Click image to enlarge)