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Although treatment with IFN-gamma strongly induced the activation of STAT1 as a transcriptional activator, its target molecule, IRF1, was not clearly produced in Lmp2-deficient uterine smooth muscle cells.
down-regulation of IL-33 protein levels by IFN-gamma in pulmonary fibroblasts and in the lungs in vivo occurs through STAT1 and non-canonical use of the LMP2 proteasome
Data show that knockdown of i-proteasome catalytic subunit PSMB9 by short hairpin RNA (shRNA) decreased the expression of both PSMB9 and PSMB8 without affecting other catalytic subunits of the proteasome.
LMP2 has a role as a tumor-suppressor and may have a role in uterine leiomyosarcoma therapy
In this study, we have identified how LMP2 can exert its function in Ag processing
Mixed proteasomes present in LMP2-deficient mice compromise virtually every parameter of the immune response against influenza A virus, potentially through dysregulation of signaling pathways, such as the nuclear factor (NF)-kappaB pathway.
Development of spontaneous uterine tumors in low molecular mass polypeptide-2 knockout mice.
The presence of immuno subunits in nonimmune tissues such as lens suggests that the immunoproteasome may also have nonimmune functions, such as that in lens differentiation.
Comparison of LMP2 KO mice and non-transgenic mice of the same background show that LMP2 KO mice exhibit a higher degree of motor function, but possess a similar level of cognitive function and ambulation.
Immunoproteasome LMP2 can at least in part determine subdominance and shape the epitope hierarchy of cytotoxic T cell responses in vivo.
Immunoproteasome LMP2 may affect CD8+ T cell responses to only a limited number of viral epitopes; its main biological function may lie elsewhere.
These results demonstrate the ability of the IFN-induced proteasome catalytic subunits to shape the HBV-specific CD8 T-cell response and thus potentially influence the progression of infection to acute or chronic disease.
two inducible subunits of the proteasome, lmp2 and lmp7, are transcriptionally up-regulated by heat shock; heat-shocked cells show enhanced presentation of immunoproteasome-dependent MHC I antigenic epitopes, but not immunoproteasome-independent epitopes
SOD1/LMP2-/- mice show no change in motor function decline, or survival compared to G93A SOD1 mice, suggesting that the loss of immuno-proteasome function in vivo does not significantly alter mutant SOD1-induced disease.
LMP-2 is required for normal proteasomal function and ischemic preconditioning induction in the heart. Its action may be related to PTEN protein degradation.
Defective PSMB9/beta1i expression is likely to be one of the risk factors for the development of human uterine neoplasm.
single nucleotide polymorphism in PSMB9 are associated with hand dermatitis
Data show that tight junction protein 1 (TJP1) suppressed expression of the catalytically proteasome subunits LMP7 and LMP2, decreased proteasome activity, and enhanced proteasome inhibitor sensitivity in vitro and in vivo through suppression of EGFR/JAK1/STAT3 signaling.
Chinese females carrying the rs17587-G/G genotype in PSMB9 may increase a higher risk for Parkinson's disease.
designed siRNAs that efficiently silence LMP2, LMP7 and MECL-1 gene expression.
The TAP1-rs1135216 and PSMB9-rs17587 variants are significantly associated with vitiligo, and even one copy of these mutant alleles can influence the risk among Saudis.
Comparison with reference profiles of sorted immune cells and healthy muscle confirmed upregulation of PSMB8 and -9 in myositis biopsies beyond infiltration related changes.
study found prevalence of LMP2-AA genotype was higher in acute myeolid leukemia (AML) patients while it was significantly lower in multiple myeloma (MM) cases than in the control subjects; results suggestLMP2 polymorphisms could play a role in the development of AML and MM
Data indicate that the codon 60 Arg/His polymorphism does not significantly alter the expression and activity of beta1i among the cell lines tested and clinical samples from colon and pancreatic cancer.
The data show that LMP2 and PSMA6 gene polymorphism is not a risk factor of ischemic stroke in Ukrainian population.
functional variants in PSMB9 may contribute to melanoma susceptibility.
Genetic polymorphisms of rs17587 of PSMB9 appeared to be associated with rheumatoid arthritis in ethnic Han Chinese from Yunnan.
study reports expression of LMP2 in patients with renal oncocytomas (RO) and eosinophilic variant of chromophobe renal cell carcinomas (CHRCC-EO); all CHRCC-EO cases (7 of 7) strongly showed nuclear LMP2 staining, as opposed to only 2 of 56 ROs; suggest its use as an aid in differential diagnosis of these neoplasias
LMP2 expression in nasopharyngeal carcinoma is associated with poor prognosis.
In patients with primary Sjogren's syndrome, the expression of LMP7 (but not LMP2) is up-regulated in the labial gland.
Data indicate that treatment-emergent resistance to single-agent bortezomib was independent of variants in the proteasome genes PSMB1, PSMB5, PSMB6, PSMB8, PSMB9, and PSMB10.
The polymorphic site is unique in the Chinese population of Han nationality at the LMP2 codon 60 loci (Arg60Cys), but a lack of association with lung cancer exists.
The MAGE-C(2336-344) antigenic peptide is produced by the immunoproteasome and intermediate proteasome beta1i-beta5i, but not by the standard proteasome nor intermediate proteasome beta5i.
LMP2 may negatively regulate LMS independently of its role in the proteasome.
These results suggest LMP2/LMP7 gene should be regarded as molecular marker to estimate animal's immune status for their effects on hematological traits.
LMP2 is involved in antigen presentation and is an important candidate gene for initial exploration of relationships between antigen processing genes and disease resistance.
The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits\; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit.
proteasome (prosome, macropain) subunit, beta type, 9 (large multifunctional peptidase 2)
, proteasome beta subunit
, proteasome beta 9 subunit
, Low molecular mass protein 2
, proteasome subunit beta type-9
, proteasome subunit, beta type 9
, proteasome subunit beta type-9b
, low molecular mass protein 2b
, large multifunctional protease 2
, low molecular mass protein 2
, macropain chain 7
, multicatalytic endopeptidase complex chain 7
, proteasome chain 7
, proteasome subunit beta-1i
, proteosome (prosome, macropain) subunit, beta type 9 (large multifunctional peptidase 2)
, proteosome beta 9 subunit
, really interesting new gene 12 protein
, large multifunctional peptidase 2
, proteasome catalytic subunit 1i
, proteasome subunit beta 6i
, proteasome-related gene 2
, proteasome (prosome, macropain) subunit, beta type, 9 (large multifunctional protease 2)
, RING12 protein
, low molecular mass polypeptide 2
, proteasome (prosome, macropain) subunit, beta type 9 (large multifunctional peptidase 2)
, proteosome (prosome, macropain) subunit, beta type 9
, proteasome subunit, beta type 9 (large multifuntional protease 2)
, proteasome (prosome, macropain) subunit, beta type, 9a
, Proteasome subunit beta type-9
, low molecular mass polypeptide complex subunit 2