Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: > 80% SDS-PAGE
- Active: Yes
- Tags: GST tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant human KMT3C / SMYD2 protein (Active)
See all KMT3C / SMYD2 proteins and peptides
The specific activity of ab268975 was 160 pmol/min/mg in a methyltransferase assay using histone H3 peptide (1-21) as substrate.
Purity> 80 % SDS-PAGE.
Expression systemBaculovirus infected Sf9 cells
Protein lengthFull length protein
Molecular weight information70 kDa by SDS-PAGE
TagsGST tag N-Terminus
Our Abpromise guarantee covers the use of ab268975 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.79% Tris HCl, 0.29% Sodium chloride, 0.31% Glutathione, 0.003% EDTA, 0.004% DTT, 0.002% PMSF, 25% Glycerol (glycerin, glycerine)
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Histone methyltransferase SMYD2
- HSKM B
FunctionProtein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.
Sequence similaritiesContains 1 MYND-type zinc finger.
Contains 1 SET domain.
Cellular localizationCytoplasm > cytosol. Nucleus.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab268975 has not yet been referenced specifically in any publications.