Product Pathways - Chromatin Regulation / Epigenetics
SMYD3 (D2Q4V) Rabbit mAb #12859
|12859S||100 µl (10 western blots)||---||In Stock||---|
|12859||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Monkey||Endogenous||42||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
SMYD3 (D2Q4V) Rabbit mAb recognizes endogenous levels of total SMYD3 protein. This antibody does not cross-react with other SMYD proteins.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro357 of human SMYD3 protein.
SET and MYND domain containing protein 3 (SMYD3) is a member of the SET domain-containing family of protein methyltransferases and is localized to both the nucleus and cytoplasm (1-3). Several histone substrates have been identified for SMYD3; however, the data is controversial. In one study, SMYD3 has been shown to methylate histone H3 Lys4 (both di- and tri-methylation) and interact with RNA polymerase II to activate transcription (1). A second study has shown that SMYD3 preferentially methylates histone H4 Lys20 and interacts with nuclear receptor corepressor complex (NCOR) to repress transcription (2). A third study has shown that SMYD3 preferentially methylates histone H4 Lys5 (mono-, di-, and tri-methylation) (3). In addition, SMYD3 has been shown to methylate the endothelial growth factor receptor 1 (VEGFR1) on Lys831 and stimulate its kinase activity (4). Regardless of the preferred protein substrates, it is clear that SMYD3 functions as an oncogene. Research studies have shown SMYD3 is highly over-expressed in liver, breast, and rectal carcinomas. Over-expression of SMYD3 in multiple cell lines enhances proliferation, adhesion, and migration, while reduced expression results in significant suppression of cell growth (1,5-10). In addition, multiple cancer cell lines express both full length SMYD3 and a cleaved form of SMYD3 lacking the N-terminal 34 amino acids, and the cleaved form shows increased methyltransferase activity toward histone H3 (11).
- Hamamoto, R. et al. (2004) Nat Cell Biol 6, 731-40.
- Foreman, K.W. et al. (2011) PLoS One 6, e22290.
- Van Aller, G.S. et al. (2012) Epigenetics 7, 340-3.
- Kunizaki, M. et al. (2007) Cancer Res 67, 10759-65.
- Luo, X.G. et al. (2007) J Biosci Bioeng 103, 444-50.
- Wang, S.Z. et al. (2008) BMB Rep 41, 294-9.
- Zou, J.N. et al. (2009) Cancer Lett 280, 78-85.
- Luo, X.G. et al. (2009) IUBMB Life 61, 679-84.
- Luo, X.G. et al. (2010) IUBMB Life 62, 194-9.
- Ren, T.N. et al. (2011) Med Oncol 28 Suppl 1, S91-8.
- Silva, F.P. et al. (2008) Oncogene 27, 2686-92.
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For Research Use Only. Not For Use In Diagnostic Procedures.