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The protein encoded by TRIM22 is a member of the tripartite motif (TRIM) family. Additionally we are shipping TRIM22 Antibodies (67) and TRIM22 Kits (3) and many more products for this protein.
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Data show that RNA interference abolished IFN-gamma-induced (show SAMHD1 Proteins) TRIM22 expression, indicating an IRF-1 (show IRF1 Proteins)-dependent expression of TRIM22.
Study shows that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain.
Infant with severe IBD characterized by granulomatous colitis and severe perianal disease, we identified a homozygous variant of TRIM22 that affects the ability of its product to regulate NOD2.
Interferon-alpha (show IFNA Proteins)-induced TRIM22 interrupts hepatitis c virus replication by ubiquitinating NS5A.
regulation of FoxO4 (show FOXO4 Proteins) protein expression and cell survival by TRIM22 controls TLR3 (show TLR3 Proteins)-mediated IFN type I gene induction, preventing excessive antiviral response through dsRNA-induced apoptosis.
TRIM22 could interact with IkappaB kinase (IKK)alpha (show CHUK Proteins) but not IKKbeta (show IKBKB Proteins) and could increase the level and phosphorylation of IKKalpha (show CHUK Proteins) through its really interesting new gene (RING) and spla-ryanodine receptor (show RYR3 Proteins) (SPRY) domains.
Demonstrated that TRIM22 acts as a negative regulator of HIV-1 replication via inhibition of basal Sp1 (show PSG1 Proteins)-driven proviral transcription.
propose that TRIM22 is a direct target gene of PR and that it can mediate progesterone actions in uterine cells
Data show that capsid protein p24-DsRed-Monomer was co-localized with tripartite motif containing 22 (TRIM22)-EGFP in HEK293T cells.
A number of putative structural and functional residues, including several sites that undergo post-translational modification, were also identified in TRIM22.
our data characterize the extensive genetic variation in TRIM22 and identify rs1063303:G>C as a highly prevalent SNP that influences its function.
Upregulation of TRIM22 may be associated with responsiveness to Peg (show PAEP Proteins)-IFNalpha-2a/RBV combination therapy in hepatitis C.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the cytoplasm and its expression is induced by interferon. The protein down-regulates transcription from the HIV-1 LTR promoter region, suggesting that function of this protein may be to mediate interferon's antiviral effects. Alternative splicing results in multiple transcript variants.
E3 ubiquitin-protein ligase TRIM22
, tripartite motif-containing 22
, tripartite motif containing 22
, 50 kDa-stimulated trans-acting factor
, RING finger protein 94
, stimulated trans-acting factor (50 kDa)
, tripartite binding motif 22
, tripartite motif protein TRIM22
, tripartite motif-containing protein 22