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Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Additionally we are shipping SMYD2A Antibodies (72) and SMYD2A Proteins (14) and many more products for this protein.
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Lysine methylation represses p53 activity in teratocarcinoma cancer cells via up-regulation of SMYD2 and PR-Set7 and perpetuation of cancer cells proliferation.
SMYD2-H4K20me1-L3MBTL1 axis contributes to HIV-1 latency and can be targeted with small-molecule SMYD2 inhibitors.
identifie novel cellular substrates of the lysine methyltransferase SMYD2. Of the 14 novel putative SMYD2 substrates identified, six were confirmed in cells by immunoprecipitation: MAPT, CCAR2, EEF2, NCOA3, STUB1, and UTP14A. Treatment with the selective SMYD2 inhibitor BAY-598 abrogated the methylation signal, indicating that methylation of these novel substrates was dependent on the catalytic activity of SMYD2
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-ALK gene significantly attenuated the phosphorylation levels of the EML4-ALK protein.
SMYD2 knockdown confers relative resistance to human AML (show RUNX1 ELISA Kits) cells against multiple classes of DNA damaging agents.
Substrate crevices of Smyd2 and Smyd3 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, and NO66 in renal cell tumors. Their low expression levels were significantly associated with shorter disease-specific and disease-free survival.
Our data indicate that Smyd2 has a critical role downstream of Myc (show MYC ELISA Kits) in acute myeloid leukemia (show BCL11A ELISA Kits)
two positive feedback loops that integrate epigenetic regulation and renal inflammation in cyst development: SMYD2/IL-6/STAT3/SMYD2 and SMYD2/TNF-alpha/NF-kappaB/SMYD2.
a pivotal role for SMYD2 in promoting pancreatic cancer.
Data show that histone methyltransferase Smyd2 inhibits macrophage interleukin 6 (IL-6 (show IL6 ELISA Kits)) and tumor necrosis factor alpha (TNF-alpha (show TNF ELISA Kits)) 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, interacts with RNA Polymerase II as well as to the RNA helicase, HELZ (show HELZ ELISA Kits)
Sin3A-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 ELISA Kits)-responsive genes in a p53 (show TP53 ELISA Kits)-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
N-lysine methyltransferase SMYD2
, SET and MYND domain-containing protein 2
, histone methyltransferase SMYD2
, lysine N-methyltransferase 3C
, zinc finger, MYND domain containing 14
, HSKM-B protein
, Histone methyltransferase SMYD2-A
, N-lysine methyltransferase SMYD2-A
, SET and MYND domain-containing protein 2A
, SET and MYND domain containing 2
, histone methyltransferase SMYD2-A
, Histone methyltransferase SMYD2
, SET and MYND domain-containing 2