Protein-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.
Contains 1 MYND-type zinc finger. Contains 1 SET domain.
All lanes : Anti-KMT3C / SMYD2 antibody (ab108217) at 0.1 µg/ml
Lane 1 : HeLa whole cell
lysate at 50 µg Lane 2 : HeLa whole cell
lysate at 15 µg Lane 3 : HeLa whole cell
lysate at 5 µg Lane 4 : 293T whole cell
lysate at 50 µg Lane 5 : NIH 3T3 whole cell
lysate at 50 µg
Developed using the ECL technique
Predicted band size : 50 kDa
Exposure time : 3 minutes
Western blot - Anti-KMT3C / SMYD2 antibody (ab108217)This image is courtesy of an anonymous Abreview
All lanes : Anti-KMT3C / SMYD2 antibody (ab108217) at 1/1000 dilution
Detection of KMT3C / SMYD2 by Western blot of Immunprecipitate.
ab108217, at 1 µg/ml, staining KMT3C / SMYD2 in HeLa whole cell lysate immunoprecipitated using ab108217 at 6 µg/mg lysate (1 mg/IP; 20% of IP loaded/lane). Detection: Chemiluminescence with an exposure time of 10 seconds.
Xu G et al. The histone methyltransferase Smyd2 is a negative regulator of macrophage activation by suppressing interleukin 6 (IL-6) and tumor necrosis factor a (TNF-a) production. J Biol Chem290:5414-23 (2015).
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