Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

SMYD2 Antibody #4251

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk (B) (Pg) Endogenous 49 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  B=Bovine  Pg=Pig
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 Antibody detects endogenous levels of total SMYD2 protein. The antibody does not cross-react with SMYD3 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human SMYD2 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using SMYD2 Antibody.

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).

  1. Brown, M.A. et al. (2006) Mol Cancer 5, 26.
  2. Abu-Farha, M. et al. (2008) Mol Cell Proteomics 7, 560-72.
  3. Huang, J. et al. (2006) Nature 444, 629-32.
  4. 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.

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