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The protein encoded by RNF128 is a type I transmembrane protein that localizes to the endocytic pathway. Additionally we are shipping Ring Finger Protein 128 Antibodies (48) and many more products for this protein.
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loss of Grail enhances anti-tumour reactivity and functionality of CD8 (show CD8A Proteins)(+) T cells.
GRAIL expression is regulated by the IL2 (show IL2 Proteins)/mTOR (show FRAP1 Proteins)/Otubain-1 (show OTUB1 Proteins) axis in CD4 (show CD4 Proteins) T cells during Trypanosoma cruzi infection.
this study identified RNF128 as an E3 ligase for K63-linked ubiquitination and activation of TBK1 (show TBK1 Proteins) to RNA and DNA viruses
Grail plays a critical role in controlling Th2 cell development through a negative feedback loop by targeting STAT6 (show STAT6 Proteins) for degradation.
GRAIL-expressing T cells expressed regulatory T cell markers and showed suppressive effects in murine dextran sodium salt-induced colitis.
findings reveal a novel association of the increased GRAIL expression with impaired CD4 (show CD4 Proteins) T cell proliferation
Data reveal that GRAIL regulates proteins involved in the actin cytoskeletal organization, thereby maintaining the unresponsive state of anergic T cells.
GRAIL, by mediating TCR-CD3 (show CD3E Proteins) degradation, regulates naive T cell tolerance induction and Treg cell function
a biochemical pathway composed of GRAIL and/or GRAIL-interacting proteins is important in the development of the CD4 (show CD4 Proteins) T cell anergic phenotype in vivo.
Down-regulation of CD40L (show CD40LG Proteins) occurred following ectopic expression of GRAIL in naive T cells from CD40 (show CD40 Proteins)(-/-) mice
results show that expression of GRAIL is uniquely regulated by the specific miRNA in intestinal mucosa, and suggest that GRAIL may associate with the pathophysiology of Crohn's disease
study shows that Grail has a novel, p53 (show TP53 Proteins)-dependent role in regulating the cell cycle and apoptosis
Forced expression of GRAIL in a T cell line from a T-cell receptor transgenic mouse is sufficient for conversion of these cells to a regulatory phenotype.
Inhibition of T cell activation is not due to apoptosis or disruption of proximal T- cell receptor signaling, but is associated with up-regulation of GRAIL in CD4+ T cells, with modest effects on other E3 ubiquitin ligases.
GRAIL expression was significantly higher in patients with ulcerative colitis in remission than in patients with active disease and in healthy volunteers.
GRAIL captures and then ubiquitinates transmembrane proteins across the cell membrane
endogenous GRAIL regulates general cell cycle and proliferation of primary naive CD4 (show CD4 Proteins) T cells.
GRAIL can down-modulate the expression of CD83 antigen (show CD83 Proteins) on CD4 (show CD4 Proteins) T cells.
The protein encoded by this gene is a type I transmembrane protein that localizes to the endocytic pathway. This protein contains a RING zinc-finger motif and has been shown to possess E3 ubiquitin ligase activity. Expression of this gene in retrovirally transduced T cell hybridoma significantly inhibits activation-induced IL2 and IL4 cytokine production. Induced expression of this gene was observed in anergic CD4(+) T cells, which suggested a role in the induction of anergic phenotype. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
E3 ubiquitin-protein ligase RNF128
, ring finger protein 128
, gene related to anergy in lymphocytes protein
, goliath-related E3 ubiquitin-protein ligase 1
, goliath-related E3 ubiquitin ligase 1