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SET domain-containing proteins, such as SMYD2, catalyze lysine methylation (Brown et al., 2006. Additionally we are shipping SET and MYND Domain Containing 2 Proteins (12) and SET and MYND Domain Containing 2 Kits (1) and many more products for this protein.
Showing 10 out of 69 products:
Human Polyclonal SMYD2 Primary Antibody for ELISA, WB - ABIN4369823
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
Show all 2 Pubmed References
Cow (Bovine) Polyclonal SMYD2 Primary Antibody for ChIP, WB - ABIN2784266
Shibamoto, Ogino, Suzuki, Takemoto, Araki, Isobe, Tsuchida, Nakamura, Kenjo, Suzuki, Hosono, Tokumaru, Ishihara, Kato, Ii, Hayabuchi: Primary central nervous system lymphoma in Japan: changes in clinical features, treatment, and prognosis during 1985-2004. in Neuro-oncology 2008
Show all 2 Pubmed References
The SMYD2 may promote BMP signaling by directly methylating BMPR2, which, in turn, stimulates BMPR2 kinase activity and activation of the BMP pathway.
Knockdown of SMYD2 as well as treatment with a SMYD2 inhibitor in two NSCLC cell lines with an EML4 (show EML4 Antibodies)-ALK (show ALK Antibodies) gene significantly attenuated the phosphorylation levels of the EML4 (show EML4 Antibodies)-ALK (show ALK Antibodies) protein.
SMYD2 knockdown confers relative resistance to human AML (show RUNX1 Antibodies) cells against multiple classes of DNA damaging agents.
Substrate crevices of Smyd2 and Smyd3 (show SMYD3 Antibodies) show distinct features in terms of spatial, hydration, and electrostatic properties that emphasize their characteristic modes of substrates interaction and entry pathways for inhibitor binding.
High expression of SMYD2 is associated with chronic lymphocytic leukemia.
Study reveals a collection of 10 enriched sequence motifs in Kme1 sites that were identified upon SMYD2 overexpression which were also downregulated in response to SMYD2 knockdown. These findings suggest that these motifs reflect the substrate specificity of SMYD2 in esophageal squamous cell carcinoma cell line.
Results show that high expression levels of SMYD2, SETD3 (show SETD3 Antibodies), and NO66 (show C14orf169 Antibodies) in renal cell tumors. Their low expression levels were significantly associated with shorter disease-specific and disease-free survival.
Suggest that SMYD2 plays a role in tumor progression and might be a useful prognosticator in HPV-unrelated, nonmultiple head and neck squamous cell carcinomas.
SMYD2-mediated methylation negatively regulates PTEN (show PTEN Antibodies) tumor suppressor activity and results in activation of the phosphatidylinositol 3-kinase-AKT (show AKT1 Antibodies) pathway.
Comprehensive motif-based searches and mutational analysis further established four additional substrates of SMYD2.
two positive feedback loops that integrate epigenetic regulation and renal inflammation in cyst development: SMYD2/IL-6 (show IL6 Antibodies)/STAT3 (show STAT3 Antibodies)/SMYD2 and SMYD2/TNF-alpha (show TNF Antibodies)/NF-kappaB (show NFKB1 Antibodies)/SMYD2.
a pivotal role for SMYD2 in promoting pancreatic cancer.
Data show that histone methyltransferase Smyd2 inhibits macrophage interleukin 6 (IL-6 (show IL6 Antibodies)) and tumor necrosis factor alpha (TNF-alpha (show TNF Antibodies)) production. production.
Smyd2 is a lysine methyltransferase which has, next to its nuclear activity, specific regulatory functions in the cytoplasm of heart and skeletal muscle cells.
Smyd2, similar to Smyd3 (show SMYD3 Antibodies), interacts with RNA Polymerase II as well as to the RNA helicase, HELZ (show HELZ Antibodies)
Sin3A (show SIN3A Antibodies)-mediated deacetylation within the coding regions of active genes is directly linked to the histone methyltransferase activity of Smyd2 [Symd2]
results show that Smyd2 negatively regulates p53 (show TP53 Antibodies)-responsive genes in a p53 (show TP53 Antibodies)-dependent manner
Findings suggest that SMYD2 (SET and MYND domain containing protein 2), a histone lysine methyltransferase, plays a critical role at early stages of development.
SET domain-containing proteins, such as SMYD2, catalyze lysine methylation (Brown et al., 2006
SET and MYND domain containing 2
, SET and MYND domain-containing protein 2-like
, N-lysine methyltransferase SMYD2
, SET and MYND domain-containing protein 2
, histone methyltransferase SMYD2
, lysine N-methyltransferase 3C
, zinc finger, MYND domain containing 14
, Histone methyltransferase SMYD2
, SET and MYND domain-containing 2
, HSKM-B protein
, Histone methyltransferase SMYD2-A
, N-lysine methyltransferase SMYD2-A
, SET and MYND domain-containing protein 2A
, histone methyltransferase SMYD2-A