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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. Zusätzlich bieten wir Ihnen TRIM37 Proteine (4) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal TRIM37 Primary Antibody für IP, WB - ABIN252974
Tabah, Tardif, Mansky: Anti-HIV-1 activity of Trim 37. in The Journal of general virology 2014
TRIM37 mutation is associated with mulibrey nanism.
TRIM37-mediated ubiquitylation stabilizes PEX5 (zeige PEX5 Antikörper) and promotes peroxisomal matrix protein import, suggesting that mulibrey nanism is a new peroxisomal biogenesis disorder.
TRIM37 was overexpressed in human CRC (zeige CALR Antikörper) tissues. High TRIM37 expression resulted in increased CRC (zeige CALR Antikörper) proliferation, migration and invasion. Mechanistically, it was confirmed that TRIM37 enhanced invasion and metastasis of CRC (zeige CALR Antikörper) via the epithelialmesenchymal transition pathway.
knockdown of TRIM37 markedly downregulated the expression of beta-catenin (zeige CTNNB1 Antikörper), cyclin D1 (zeige CCND1 Antikörper), and c-Myc (zeige MYC Antikörper) in CRC (zeige CALR Antikörper) cells. These results suggest that knockdown of TRIM37 inhibits proliferation and tumorigenesis by the inactivation of Wnt (zeige WNT2 Antikörper)/beta-catenin (zeige CTNNB1 Antikörper) signaling in CRC (zeige CALR Antikörper) 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 (zeige FAM126A Antikörper) and a candidate target for HCC (zeige FAM126A Antikörper) 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.
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 (zeige AIF1 Antikörper) 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