Human TRIM33 peptide

Name: Human TRIM33 peptide
SKU: DAG-P1231
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

18 amino acids near the center of human TRIM33.

Purity

> 95 % by SDS-PAGE.

Format

Lyophilized

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Reconstitution

TRIM33 peptide is supplied as 1mg of dried peptide. When the peptide is reconstituted in 1 mL strile water, the concentration will be 1 mg/mL.

Introduction

The protein encoded by this gene is thought to be a transcriptional corepressor. However, molecules that interact with this protein have not yet been identified. The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined. [provided by RefSeq, Jul 2008]

Entrez Gene ID

51592

Synonyms

TRIM33; tripartite motif containing 33; ECTO; PTC7; RFG7; TF1G; TIF1G; TIFGAMMA; TIF1GAMMA; E3 ubiquitin-protein ligase TRIM33; TIF1-gamma; protein Rfg7; ectodermin homolog; RET-fused gene 7 protein; tripartite motif-containing 33; transcriptional intermediary factor 1 gamma;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Knockdown of miR-629 Inhibits Ovarian Cancer Malignant Behaviors by Targeting Testis-Specific Y-Like Protein 5

DNA AND CELL BIOLOGY

Authors: Shao, Liping; Shen, Zongji; Qian, Hua; Zhou, Sufang; Chen, Youguo

Abstract

Ovarian cancer (OC) is the most lethal gynecological cancer. The molecular mechanism of it is complicated, and numerous researches suggest that microRNAs are key regulators for it. This study was to investigate the pivotal role of miR-629 in the progression of OC and to reveal the possible molecular mechanism of its action. Testis-specific Y-like protein 5 (TSPYL5) is a tumor suppressor gene in various cancers, but there is little for its role in OC. OC OVCAR3 cells were transfected with the miR-629 vector, miR-629 inhibitor, and/or small interfering RNA (siRNA) targeting TSPYL5 (si-TSPYL5), respectively. After transfection, cell apoptosis, the ability of migration, and invasion were explored, as well as the level of miR-629 and TSPYL5 protein expression were detected by quantitative polymerase chain reaction and western blot. Compared with the control, there was increasing of miR-629, and decreasing of TSPYL5 and caspase 3 in OC tissue. Overexpression of miR-629 promoted the cell ability of migration and invasion and reduced OC cell apoptosis. In addition, elevated cancer inhibition ability of TSPYL5 induced by the miR-629 inhibitor was significantly blocked by inhibition of TSPYL5 (si-TSPYL5). All the above results suggested that miR-629 could promote OC proliferation, migration, and invasion by directly suppressing TSPYL5 expression, and inhibition of miR-629 might serve as a therapeutic target for OC.

Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Authors: Herquel, Benjamin; Ouararhni, Khalid; Khetchoumian, Konstantin; Ignat, Mihaela; Teletin, Marius; Mark, Manuel; Bechade, Guillaume; Van Dorsselaer, Alain; Sanglier-Cianferani, Sarah; Hamiche, Ali; Cammas, Florence; Davidson, Irwin; Losson, Regine

Abstract

TRIM24 (TIF1 alpha), TRIM28 (TIF1 beta), and TRIM33 (TIF1 gamma) are three related cofactors belonging to the tripartite motif superfamily that interact with distinct transcription factors. TRIM24 interacts with the liganded retinoic acid (RA) receptor to repress its transcriptional activity. Germ line inactivation of TRIM24 in mice deregulates RA-signaling in hepatocytes leading to the development of hepatocellular carcinoma (HCC). Here we show that TRIM24 can be purified as at least two macromolecular complexes comprising either TRIM33 or TRIM33 and TRIM28. Somatic hepatocyte-specific inactivation of TRIM24, TRIM28, or TRIM33 all promote HCC in a cell-autonomous manner in mice. Moreover, HCC formation upon TRIM24 inactivation is strongly potentiated by further loss of TRIM33. These results demonstrate that the TIF1-related subfamily of TRIM proteins interact both physically and functionally to modulate HCC formation in mice.