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TRIM37 encodes a member of the tripartite motif (TRIM) family, whose members are involved in diverse cellular functions such as developmental patterning and oncogenesis. Additionally we are shipping TRIM37 Proteins (4) and many more products for this protein.
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Human Polyclonal TRIM37 Primary Antibody for IP, WB - ABIN252974
Tabah, Tardif, Mansky: Anti-HIV-1 activity of Trim 37. in The Journal of general virology 2014
Human Polyclonal TRIM37 Primary Antibody for ELISA, WB - ABIN184830
Avela, Lipsanen-Nyman, Idänheimo, Seemanová, Rosengren, Mäkelä, Perheentupa, Chapelle, Lehesjoki: Gene encoding a new RING-B-box-Coiled-coil protein is mutated in mulibrey nanism. in Nature genetics 2000
TRIM37 was overexpressed in human CRC (show CALR Antibodies) tissues. High TRIM37 expression resulted in increased CRC (show CALR Antibodies) proliferation, migration and invasion. Mechanistically, it was confirmed that TRIM37 enhanced invasion and metastasis of CRC (show CALR Antibodies) via the epithelialmesenchymal transition pathway.
knockdown of TRIM37 markedly downregulated the expression of beta-catenin (show CTNNB1 Antibodies), cyclin D1 (show CCND1 Antibodies), and c-Myc (show MYC Antibodies) in CRC (show CALR Antibodies) cells. These results suggest that knockdown of TRIM37 inhibits proliferation and tumorigenesis by the inactivation of Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) signaling in CRC (show CALR Antibodies) cells.
The oncogenic roles of TRIM37 in pancreatic cancer.
These finding may provide insight into the understanding of TRIM37 as a novel critical factor of HCC (show FAM126A Antibodies) and a candidate target for HCC (show FAM126A Antibodies) treatment.
results reveal TRIM37 as an oncogenic H2A ubiquitin ligase that is overexpressed in a subset of breast cancers and promotes transformation by facilitating silencing of tumour suppressors and other genes.
In this study, authors demonstrate that human Trim 37 possesses anti-HIV-1 activity.
The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein: classification of mulibrey nanism as a new peroxisomal disorder
The TRIM37 acts as a TRIM domain-dependent E3 ubiquitin ligase and imply defective ubiquitin-dependent degradation of an as-yet-unidentified target protein in the pathogenesis of mulibrey nanism.
Functional link of TRIM37 to the ubiquitin-proteosome pathway may provide novel clues to the development of metabolic syndrome.
TRIM37 expression is regulated by several mechanisms: through nonsense surveillance of non-functional transcripts, as well as through 3'UTR (show UTS2R Antibodies) regulatory sequences and/or naturally occurring antisense RNAs especially in testis.
Trim37 deficiency in mouse lead to infertility, prenatal-onset growth failure, infertility, cardiopathy, risk for tumors, fatty liver, and type 2 diabetes.
We here show that the mouse Trim37 gene presents several alternative splice variants, including a testis-specific (show AIF1 Antibodies) transcript with an additional 3' exon.
This gene encodes a member of the tripartite motif (TRIM) family, whose members are involved in diverse cellular functions such as developmental patterning and oncogenesis. The TRIM motif includes zinc-binding domains, a RING finger region, a B-box motif and a coiled-coil domain. The RING finger and B-box domains chelate zinc and might be involved in protein-protein and/or protein-nucleic acid interactions. The gene mutations are associated with mulibrey (muscle-liver-brain-eye) nanism, an autosomal recessive disorder that involves several tissues of mesodermal origin. Alternatively spliced transcript variants encoding the same protein have been identified.
E3 ubiquitin-protein ligase TRIM37
, tripartite motif protein 37
, tripartite motif-containing 37
, tripartite motif-containing 37 protein
, tripartite motif-containing protein 37
, E3 ubiquitin-protein ligase TRIM37-like
, tripartite motif containing 37
, RING-B-box-coiled-coil protein
, mulibrey nanism protein
, TRAF encompassing factor 3