Product Pathways - Chromatin Regulation / Epigenetics
SMYD2 (D14H7) Rabbit mAb #9734
PhosphoSitePlus® protein, site, and accession data: SMYD2
| Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
|---|---|---|---|---|
| W IP | H M R Mk (Hm) (B) (Dg) (Hr) | Endogenous | 49 | Rabbit IgG |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
M=Mouse
R=Rat
Hm=Hamster
Mk=Monkey
B=Bovine
Dg=Dog
Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
Specificity / Sensitivity
SMYD2 (D14H7) Rabbit mAb recognizes endogenous levels of total SMYD2 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val414 of human SMYD2 protein. This antibody is not predicted to cross-react with other SMYD proteins.
Background
SET and MYND domain-containing protein 2 (SMYD2), also known as lysine methyltransferase protein 3C (KMT3C), is a member of the SMYD family of protein methyltransferases (1). All five members of this family (SMYD1, SMYD2, SMYD3, SMYD4, and SMYD5) contain a conserved catalytic SET domain, originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins. This domain is split by the MYN domain/zinc finger motif believed to facilitate protein-protein interactions (1). SMYD2 localizes to both the cytoplasm and nucleus, and is highly expressed in the adult mouse heart, brain, liver, kidney, thymus, and ovary, as well as in the developing mouse embryo (1). SMYD2 functions to repress transcription by interacting with the Sin3A repressor complex and methylating Lys36 of histone H3 (1). SMYD2 also interacts with HSP90α and methylates Lys4 of histone H3, a mark associated with transcriptional activation (2). In addition to histones as methyl substrates, SMYD2 methylates p53 at Lys370 to repress p53-mediated transcriptional activation and apoptosis (3,4).
- Brown, M.A. et al. (2006) Mol Cancer 5, 26.
- Abu-Farha, M. et al. (2008) Mol Cell Proteomics 7, 560-72.
- Huang, J. et al. (2006) Nature 444, 629-32.
- Huang, J. et al. (2007) Nature 449, 105-8.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.