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SMYD3 encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Additionally we are shipping SMYD3 Proteins (8) and many more products for this protein.
Showing 10 out of 60 products:
Human Polyclonal SMYD3 Primary Antibody for EIA, WB - ABIN453382
Zou, Wang, Yang, Luo, Xie, Xi: Knockdown of SMYD3 by RNA interference down-regulates c-Met expression and inhibits cells migration and invasion induced by HGF. in Cancer letters 2009
Show all 5 references for ABIN453382
Cow (Bovine) Polyclonal SMYD3 Primary Antibody for ChIP, WB - ABIN2784277
Silva, Hamamoto, Kunizaki, Tsuge, Nakamura, Furukawa: Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells. in Oncogene 2008
Human Polyclonal SMYD3 Primary Antibody for FACS, IHC (p) - ABIN391518
Barlési, Giaccone, Gallegos-Ruiz, Span, Lefesvre, Kruyt, Rodriguez: Genotype analysis of the VNTR polymorphism in the SMYD3 histone methyltransferase gene: lack of correlation with the level of histone H3 methylation in NSCLC tissues or with the risk of NSCLC. in International journal of cancer. Journal international du cancer 2008
VNTR genotype 3/3 of the SMYD3 gene was associated with the risk of ovarian cancer.
The present results suggest that NS5A interacts with SMYD3 and induces AP-1 (show FOSB Antibodies) activation, possibly by facilitating binding between HSP90 (show HSP90 Antibodies) and SMYD3. This may be a novel mechanism of AP-1 (show FOSB Antibodies) activation in HCV-infected cells.
SMYD3 physically interacts with the promoter of BCLAF1 (show BCLAF1 Antibodies) and upregulates its expression by accumulating di- and trimethylation of H3K4 at the BCLAF1 (show BCLAF1 Antibodies) locus. SMYD3 overexpression in bladder cancer cells promotes autophagy activation.
High expression of SMYD3 is associated with chronic lymphocytic leukemia.
results clearly revealed structural determinants for the substrate preference of SMYD3 and provided mechanistic insights into lysine methylation of MAP3K2 (show MAP3K2 Antibodies).
A novel HBx-interacting protein (show HBXIP Antibodies), SMYD3, was identified, leading to proposal of a novel mechanism of AP-1 (show FOSB Antibodies) activation in HBV-infected cells.
Postulate that AdoMet (show MAT1A Antibodies) cofactor acts like a key and locks Smyd3 in a closed conformation.
Results showed that SMYD3 is overexpressed in human glioma and contributes to glioma tumorigenicity through p53 (show TP53 Antibodies).
SMYD3 interacts with the human positive coactivator 4 (PC4 (show IFRD1 Antibodies)) and that such interaction potentiates a group of genes whose expression is linked to cell proliferation and invasion.
Results support a proto-oncogenic role for SMYD3 in prostate carcinogenesis, mainly due to its methyltransferase enzymatic activity.
The transcription-potentiating function of Smyd3 is restricted to a particular set of genes.
Epigenetic control of Foxp3 (show FOXP3 Antibodies) by SMYD3 H3K4 histone methyltransferase controls iTreg development and regulates pathogenic T-cell responses during pulmonary viral infection.
These findings indicate that SMYD3 plays an important role in early embryonic lineage commitment and peri (show POSTN Antibodies)-implantation development through the activation of lineage-specific genes.
represent the proof of principle that SMYD3 is a druggable target
methylation of MAP3K2 by SMYD3 increases MAP kinase signalling and promotes the formation of Ras-driven carcinomas
SMYD3 depletion prevents muscle loss and fiber size decrease; findings reveal a mechanistic link between SMYD3/BRD4 (show BRD4 Antibodies)-dependent transcriptional regulation, muscle mass determination, and skeletal muscle atrophy
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.
This gene encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Multiple transcript variants encoding different isoforms have been found for this gene.
SET and MYND domain containing 3
, SET and MYND domain-containing protein 3
, bA74P14.1 (novel protein)
, histone-lysine N-methyltransferase SMYD3
, zinc finger MYND domain-containing protein 1
, zinc finger protein, subfamily 3A (MYND domain containing), 1
, zinc finger, MYND domain containing 1
, SET and MYND domain-containing 3