TIF1 EMSA Probe Set
- Known as:
- TIF1 EMSA Probe Set
- Catalog number:
- AY1250P
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- TIF1 EMSA Probe Set
Related genes to: TIF1 EMSA Probe Set
- Gene:
- TRIM24 NIH gene
- Name:
- tripartite motif containing 24
- Previous symbol:
- TIF1
- Synonyms:
- hTIF1, Tif1a, RNF82, TIF1A
- Chromosome:
- 7q33-q34
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-18
- Date modifiied:
- 2018-02-13
- Gene:
- TRIM28 NIH gene
- Name:
- tripartite motif containing 28
- Previous symbol:
- -
- Synonyms:
- TIF1B, KAP1, TF1B, RNF96, PPP1R157
- Chromosome:
- 19q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2001-08-10
- Date modifiied:
- 2014-11-19
- Gene:
- TRIM33 NIH gene
- Name:
- tripartite motif containing 33
- Previous symbol:
- -
- Synonyms:
- TIF1GAMMA, FLJ11429, KIAA1113, TIFGAMMA, RFG7, TF1G, TIF1G, PTC7
- Chromosome:
- 1p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-08-10
- Date modifiied:
- 2016-10-05
- Gene:
- TRIM66 NIH gene
- Name:
- tripartite motif containing 66
- Previous symbol:
- C11orf29
- Synonyms:
- KIAA0298, TIF1D
- Chromosome:
- 11p15.4
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-19
- Date modifiied:
- 2018-11-22
Related products to: TIF1 EMSA Probe Set
(+) Control probe (DNA), biotinylated(+) Control probe (RNA), biotinylated(-) Control probe (DNA), biotinylated(-) Control probe (RNA), biotinylated0.2 mm, 30 cm Spacer Set
0.2 mm, 30 cm Spacer Set0.35 mm, 30 cm Spacer Set
0.35 mm, 30 cm Spacer Set0.5 mm, 30 cm Spacer Set
0.5 mm, 30 cm Spacer Set0.75 mm Dual Gel Cast Set
0.75 mm Dual Gel Cast Set0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
Related articles to: TIF1 EMSA Probe Set
- We aimed to investigate the roles of tripartite motif (TRIM) proteins in urological cancers. : A systematic review was conducted to investigate the oncological role of tripartite motif proteins in urological cancers. : A total of 84 articles were identified for the final analysis (26 articles on kidney cancers, 19 on bladder cancers, 37 on prostate cancers, and 1 on testicular cancers). In total, 27 TRIM family proteins were involved in kidney cancer, of which 9 were associated with tumor-promoting findings (TRIM24, TRIM27, TRIM37, TRIM44, TRIM46, TRIM47, TRIM59, TRIM63, and TRIM65) and of which 9 TRIM proteins were tumor-suppressive (TRIM2, TRIM7, TRIM8, TRIM13, TRIM21, TRIM26, TRIM28, TRIM33, and TRIM58). Fourteen TRIM family proteins were associated with bladder cancer (tumor-promoting: TRIM9, TRIM25, TRIM26, TRIM28, TRIM29, TRIM59, TRIM65, and TRIM66; tumor-suppressive: TRIM19 and TRIM38). Ten TRIM family proteins were associated with prostate cancer (tumor-promoting: TRIM11, TRIM24, TRIM28, TRIM33, TRIM44, TRIM59, TRIM63, TRIM66, and TRIM68; tumor-suppressive: TRIM32 and TRIM36). Twenty-eight TRIM family proteins were identified to be associated with prostate cancer (tumor-promoting: TRIM11, TRIM24, TRIM28, TRIM33, TRIM44, TRIM59, TRIM63, TRIM66, and TRIM68; tumor-suppressive: TRIM32 and TRIM36). TRIM proteins regulate urological cancers by ubiquitination or modulation of oncologic pathways. : This review identifies TRIM proteins that are involved in urological cancers. Some of these proteins have the potential to be the therapeutic target. - Source: PubMed
Publication date: 2025/07/16
Yamada YutaKimura NaokiMaki KazukiHakozaki YujiUrabe FumihikoKimura ShojiFujimura TetsuyaInoue SatoshiKume Haruki - TRIM33 is a member of the tripartite motif (TRIM) family of proteins, some of which possess E3 ligase activity and are involved in the ubiquitin-dependent degradation of proteins. Four of the TRIM family proteins, TRIM24 (TIF1α), TRIM28 (TIF1β), TRIM33 (TIF1γ) and TRIM66, contain C-terminal plant homeodomain (PHD) and bromodomain (BRD) modules, which bind to methylated lysine (KMe) and acetylated lysine (KAc), respectively. Here we investigate the differences between the two isoforms of TRIM33, TRIM33α and TRIM33β, using structural and biophysical approaches. We show that the N1039 residue, which is equivalent to N140 in BRD4(1) and which is conserved in most BRDs, has a different orientation in each isoform. In TRIM33β, this residue coordinates KAc, but this is not the case in TRIM33α. Despite these differences, both isoforms show similar affinities for H3K18Ac, and bind preferentially to H3K9MeK18Ac. We used this information to develop an AlphaScreen assay, with which we have identified four new ligands for the TRIM33 PHD-BRD cassette. These findings provide fundamental new information regarding which histone marks are recognized by both isoforms of TRIM33 and suggest starting points for the development of chemical probes to investigate the cellular function of TRIM33. - Source: PubMed
Publication date: 2022/09/13
Sekirnik Angelina RReynolds Jessica KSee LarissaBluck Joseph PScorah Amy RTallant CynthiaLee BernadetteLeszczynska Katarzyna BGrimley Rachel LStorer R IanMalattia MartaCrespillo SaraCaria SofiaDuclos StephanieHammond Ester MKnapp StefanMorris Garrett MDuarte FernandaBiggin Philip CConway Stuart J - Genomic instability is a hallmark of cancer cells which results in excessive DNA damage. To counteract this, cells have evolved a tightly regulated DNA damage response (DDR) to rapidly sense DNA damage and promote its repair whilst halting cell cycle progression. The DDR functions predominantly within the context of chromatin and requires the action of chromatin-binding proteins to coordinate the appropriate response. TRIM24, TRIM28, TRIM33 and TRIM66 make up the transcriptional intermediary factor 1 (TIF1) family of chromatin-binding proteins, a subfamily of the large tripartite motif (TRIM) family of E3 ligases. All four TIF1 proteins are aberrantly expressed across numerous cancer types, and increasing evidence suggests that TIF1 family members can function to maintain genome stability by mediating chromatin-based responses to DNA damage. This review provides an overview of the TIF1 family in cancer, focusing on their roles in DNA repair, chromatin regulation and cell cycle regulation. - Source: PubMed
Publication date: 2020/07/28
McAvera Roisin MCrawford Lisa J