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The protein encoded by USP18 belongs to the ubiquitin-specific proteases (UBP) family of enzymes that cleave ubiquitin from ubiquitinated protein substrates. Additionally we are shipping USP18 Proteins (4) and USP18 Kits (3) and many more products for this protein.
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that Ubiquitin-specific peptidase 18 directly bind to BCL2L1 (show BCL2L1 Antibodies) and positively regulated its expression in hepatocellular carcinoma cells
These findings add USP18 deficiency to the list of genetic disorders collectively termed type I interferonopathies
We show that IRF-7 (show IRF7 Antibodies) siRNA knockdown enhanced LPS (show IRF6 Antibodies)-induced IL-10 (show IL10 Antibodies) production in human monocyte-derived macrophages, and USP-18 overexpression attenuated LPS (show IRF6 Antibodies)-induced production of IL-10 (show IL10 Antibodies) in RAW264.7 cells. Quantitative PCR confirmed upregulation of USP18, USP41, IL10 (show IL10 Antibodies), and IRF7 (show IRF7 Antibodies). An independent cohort confirmed LPS (show IRF6 Antibodies) induction of USP41 and IL10 (show IL10 Antibodies) genes
results indicated that USP18 modulates the anti-HBV activity of IFN-F via activation of the JAK (show JAK3 Antibodies)/STAT (show STAT1 Antibodies) signaling pathway in Hepg2.2.15 cells.
USP18's ISG15 (show ISG15 Antibodies) specificity is mediated by a small interaction interface.
STAT2 (show STAT2 Antibodies) recruits USP18 to the type I IFN receptor subunit IFNAR2 (show IFNAR2 Antibodies) via its constitutive membrane-distal STAT2 (show STAT2 Antibodies)-binding site.
findings show that multiple inflammatory stimuli can modulate interferon (show IFNA Antibodies) stimulated gene expression and thus inhibit hepatocyte interferon (show IFNA Antibodies) signaling via USP18 induction
USP18 negatively regulates NF-kappaB (show NFKB1 Antibodies) signaling by targeting TAK1 (show MAP3K7 Antibodies) and NEMO (show IKBKG Antibodies) for deubiquitination through distinct mechanisms.
Data suggest that USP18 (Ubiquitin-like specific protease 18) sensitive cellular functions include activity of the peptide transporters PEPT1 (show SLC15A1 Antibodies) and PEPT2 (show SLC15A2 Antibodies).
Dimerization of IFNAR1 (show IFNAR1 Antibodies) and IFNAR2 (show IFNAR2 Antibodies) and the limiting role of IFNAR1 (show IFNAR1 Antibodies) binding affinity in complex assembly is modulated by USP18.
These data highlight USP18 as a host restriction factor during innate immune response to porcine respiratory and reproductive syndrome virus.
USP18 is a potential target gene that promotes reduced replication of PRRSV.
Results report identification and cloning of the ISG15 (show ISG15 Antibodies) and ISG43 genes in pig.
this study identifies the osteopenia phenotype of mice lacking Usp18, which is known as a negative regulator of type I IFN signaling
USP18 has a protective role in pathological cardiac remodeling in mouse.
Increased ISGylation was accompanied by enhanced viral resistance without causing detrimental side effects suggesting that USP18 protease inhibition might be a suitable antiviral strategy
USP18 null mice develop leiomyosarcoma recapitulating key features of clinical leiomyosarcomas and patients with reduced-USP18 tumor levels have an unfavorable outcome.
USP18 lack in microglia causes destructive interferonopathy of the mouse brain.
results suggest that increasing ISGylation by specific inhibition of USP18 protease activity could constitute a promising antiviral strategy with only a minimal risk of severe adverse effects
USP18 is crucial for IFN-gamma (show IFNG Antibodies)-mediated inhibition of B16 melanoma tumorigenesis and antitumor immunity.
Usp18-driven enforced viral replication in dendritic cells can break immunological tolerance and critically influences induction of autoimmunity.
The protein encoded by this gene belongs to the ubiquitin-specific proteases (UBP) family of enzymes that cleave ubiquitin from ubiquitinated protein substrates. It is highly expressed in liver and thymus, and is localized to the nucleus. This protein efficiently cleaves only ISG15 (a ubiquitin-like protein) fusions, and deletion of this gene in mice results in a massive increase of ISG15 conjugates in tissues, indicating that this protein is a major ISG15-specific protease. Mice lacking this gene are also hypersensitive to interferon, suggesting a function of this protein in downregulating interferon responses, independent of its isopeptidase activity towards ISG15.
ubl carboxyl-terminal hydrolase 18
, ubiquitin specific peptidase 18
, universal stress protein
, ubiquitin specific protease 18
, ubiquitin specific peptidase 41
, 43 kDa ISG15-specific protease
, ISG15-specific-processing protease
, ubl thioesterase 18
, ubl thiolesterase 18
, interferon-stimulated gene 43
, ubiquitin-specific protease 18
, ubiquitin specific protease 15