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anti-Rat (Rattus) SETD2 Antibodies:
anti-Human SETD2 Antibodies:
anti-Mouse (Murine) SETD2 Antibodies:
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Human Polyclonal SETD2 Primary Antibody for IHC, WB - ABIN5664238
Chen, Liu, Liu, Xia, Zhang, Han, Jiang, Wang, Cao: Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity. in Cell 2017
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Human Polyclonal SETD2 Primary Antibody for IHC, WB - ABIN6674472
Zhu, Lei, Ju, Wang, Huang, Yang, Shao, Zhu, Wei, Fu, Li, Wu: SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing. in Nucleic acids research 2017
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Cow (Bovine) Polyclonal SETD2 Primary Antibody for IHC, WB - ABIN2783051
Barrand, Andersen, Collas: Promoter-exon relationship of H3 lysine 9, 27, 36 and 79 methylation on pluripotency-associated genes. in Biochemical and biophysical research communications 2010
Human Polyclonal SETD2 Primary Antibody for ELISA - ABIN548025
Sun, Wei, Wu, Hu, Wang, Wang, Zhang, Chen, Huang, Chen: Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. in The Journal of biological chemistry 2005
Human Polyclonal SETD2 Primary Antibody for ICC, IF - ABIN4320758
Kanu, Grönroos, Martinez, Burrell, Yi Goh, Bartkova, Maya-Mendoza, Mistrík, Rowan, Patel, Rabinowitz, East, Wilson, Santos, McGranahan, Gulati, Gerlinger, Birkbak, Joshi, Alexandrov, Stratton, Powles et al.: SETD2 loss-of-function promotes renal cancer branched evolution through replication stress and impaired DNA repair. ... in Oncogene 2015
Study shows that monoallelic, SETD2-deficient cells retaining H3K36me3, but not alphaTubK40me3, exhibit a dramatic increase in mitotic defects and micronuclei count. In SETD2-inactivated human kidney cells rescue with a pathogenic SETD2 mutant deficient for alphaTubK40me3, but not H3K36me3 methylation, replicated this phenotype. Genomic instability was also a hallmark of patient-derived cells from clear cell renal cell...
Their overexpression induced by SETD2 knockdown caused imatinib insensitivity.
The data of this stud describe the spectrum of tumors in which SETD2 mutations are found and provide a context for interpretation of these mutations in the clinical setting.
We extensively described two additional cases with SETD2-related overgrowth. Confirmed key clinical features of SETD2-related overgrowth are macrocephaly, speech delay and behavioral problems or autism.
Our results provide evidence that SETD2 and CREB1 contribute to cisplatin cytotoxicity in non-small cell lung cancer via regulation of the ERK signaling pathway, and their inactivation may lead to cisplatin resistance.
we show a strong relationship between the expression profiles of PBRM1, BAP1 and SETD2 in ccRCC suggesting reciprocal synergy effects in the context of tumor suppression.
Proteasome inhibition rescued SETD2 expression.
SETD2 is required to maintain high H3K79 di-methylation and MLL-AF9-binding to critical target genes, such as Hoxa9.
This study of patients with ccRCC, pooled analysis and multivariable modeling demonstrated that three recurrently mutated genes, BAP1, SETD2, and TP53, have statistically significant associations with poor clinical outcomes.important clinical confounders, mutations of TP53 and SETD2 were associated with decreased CSS and RFS, respectively.
SETD2 regulates tumor growth and chemosensitivity of osteosarcoma. Overexpression of SETD2 significantly inhibited osteosarcoma cell growth in vitro and in vivo. Moreover, SETD2 significantly enhanced cisplatin-induced apoptosis in osteosarcoma cells and inhibited cancer stem cell properties in OS cells.
Finally, mutations of H3G34 or H3P38 alleviate the inhibitory effects of H3K36M on H3K36 methylation, demonstrating that the stable interaction of H3K36M with SETD2 is critical for its inhibitory effects.
H3G34/R/V/D mutations impair the catalytic activity of SETD2 due to steric clashes that impede optimal SETD2-H3K36 interaction promoting genome instability and tumorigenesis by inhibiting mismatch repair activity.
SETD2 is a potential prognostic biomarker for overall survival and progression-free survival prediction in patients with metastatic renal cell carcinoma receiving targeted therapy
This study describes SETD2 inactivation as EATL-II molecular hallmark, supports EATL-I and -II being two distinct entities, and defines potential new targets for therapeutic intervention.
PALB2 associates with active genes through its major binding partner, MRG15, which recognizes histone H3 trimethylated at lysine 36 (H3K36me3) by the SETD2 methyltransferase
SETD2 and KDM5C mutations were associated with prolonged overall survival in patients with metastatic clear cell renal cell carcinoma
SETD2 expression was decreased in gastric cancer. Low-level expression of SETD2 in patients was significantly correlated with poor prognosis. Overexpression of SETD2 inhibited proliferation, migration, and invasion significantly in Gastric Cancer cell lines.
The fusion transcript codes for a protein in which the last 114 amino acids of SETD2, i.e., the entire Set2 Rpb1 interacting (SRI) domain of SETD2, are replaced by 30 amino acids encoded by the NF1 sequence.
Our work defines SETD2 as a tumor suppressor gene in Hepatosplenic T-cell lymphoma (HSTL)and implicates genes including INO80 and PIK3CD in the disease
The findings, specifically frequent mutations of STAT5B, PIK3CD, and the histone methyltransferase SETD2, may help guide translational efforts to target hepatosplenic T-cell lymphoma
Huntington's disease (HD), a neurodegenerative disorder characterized by loss of striatal neurons, is caused by an expansion of a polyglutamine tract in the HD protein huntingtin. This gene encodes a protein belonging to a class of huntingtin interacting proteins characterized by WW motifs. This protein is a histone methyltransferase that is specific for lysine-36 of histone H3, and methylation of this residue is associated with active chromatin. This protein also contains a novel transcriptional activation domain and has been found associated with hyperphosphorylated RNA polymerase II.
histone-lysine N-methyltransferase SETD2
, kinesin family member 9
, huntingtin interacting protein 1
, huntingtin yeast partner B
, huntingtin-interacting protein B
, lysine N-methyltransferase 3A