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Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Additionally we are shipping SMYD2A Proteins (14) and SMYD2A Kits (2) and many more products for this protein.
Showing 10 out of 85 products:
Human Polyclonal SMYD2A 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 SMYD2A 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
Lysine methylation represses p53 activity in teratocarcinoma cancer cells via up-regulation of SMYD2 and PR-Set7 (show SETD8 Antibodies) 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 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.
Our data indicate that Smyd2 has a critical role downstream of Myc in acute myeloid leukemia (show BCL11A Antibodies)
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) and tumor necrosis factor alpha (TNF-alpha) 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 (show Pol II Antibodies) as well as to the RNA helicase, HELZ (show HELZ Antibodies)
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-responsive genes in a p53-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.
Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1 (By similarity).
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