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Human Polyclonal Psmd4 Primary Antibody für WB - ABIN1881698
Elangovan, Oh, Sukumaran, Wójcik, Yoo: Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13. in Biochemical and biophysical research communications 2010
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Human Polyclonal Psmd4 Primary Antibody für WB - ABIN948339
Kuzina, Kudriaeva, Smirnov, Dubina, Gabibov, Belogurov: Glatiramer acetate and nanny proteins restrict access of the multiple sclerosis autoantigen myelin basic protein to the 26S proteasome. in BioMed research international 2014
Cow (Bovine) Polyclonal Psmd4 Primary Antibody für WB - ABIN2787532
Elangovan, Choi, Jang, Kim, Yoo: The ubiquitin-interacting motif of 26S proteasome subunit S5a induces A549 lung cancer cell death. in Biochemical and biophysical research communications 2007
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Findings indicated PSMD4 as a subunit of 26S proteasome exerts as an oncogene during tumor development of hepatocellular carcinoma.
Preterm delivery is associated with low levels of anti-secretory factor in placenta. Inflammation, a potential trigger of preterm birth, is more pronounced in the preterm placenta and inversely related to the placental level of anti-secretory factor.
We therefore suggest that PSMD4 or b-catenin might be potential targets for suppressing tumor aggressiveness, and consequently, improving outcomes in patients whose tumors express cNrf2.
Binding (especially high-affinity binding) of non-ubiquitinated proteins to the Rpn10 proteasome subunit can both regulate the functioning of this proteasomal ubiquitin receptor (by competing with ubiquitinated substrates) and promote activation of other pathways for proteolytic degradation of proteins destined to the proteasome.
The platelet 26S proteasome exhibits different basal activities of its catalytic subunits and chymotrypsin-like activity is most prominently enhanced by calcium dependent signaling. Collagen stimulation enhances 26S proteasome chymotrypsin-like activity in platelets.
regulation of NY-ESO-1 processing by the ubiquitin receptors Rpn10 and Rpn13 as a well as by the standard and immunoproteasome is governed by non-canonical ubiquitination on non-lysine sites.
Not only AF1, but an entire proteasome complex, seems to be present in blood.
binds to death receptor-6, and induces monocyte cell line differentiation via NF-kB pathway
The VWA domain regulation of ubiquitin and Ubl binding to S5a is restricted to the 26S proteasome.
The degradation of TP53 and MDM2 by the proteasome can be selectively dependent on S5a in human cells.
To examine angiocidin expression in SMMC-7221 and HepG2 cells and the role of angiocidin in liver cancer cell growth. Angiocidin is highly expressed in liver cancer cells, and it may play a key role in tumor growth of liver cancers.
Authors demonstrate that human cytomegalovirus UL76 induces a novel nuclear aggresome, likely by subverting S5a of the ubiquitin-proteasome system.
One consequence of the interaction between E6/E6AP and S5a is enhanced ubiquitination of this proteasome subunit.
These studies suggest that diminished 26S activity in failing human hearts may be related ti impaired docking of the 19S to the 20S as a result of decreased Rpt subunit ATPase activity and alpha7 subunit phosphorylation.
identified the VWA domain of hRpn10 as a receptor for ubiquitin-like proteins within the 26S proteasome and elucidated how FAT10 mediates efficient proteolysis by the proteasome
Both higher PSMD4 expression levels and higher 1q21 copy numbers affected clinical outcome adversely.
results suggest that there is different substrate specificity between S5a and hRpn13 at the level of delivery and S5a may be the major docking site for ERAD substrates.
Overexpression of the S5a subunit of proteasome activator PA700 did not recover proteasome function in Huntington disease cells. S5a.
parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.
S5a component of the 19S complex interacts with different ubiquitin-like (ubl) modules
Xrpn10c-binding sites of Scythe act as an essential segment linking the ubiquitin/proteasome machinery to the control of proper embryonic development.
cloning, chromosomal localization and detection of single nucleotide polymorphisms of PSMD4
Due to differences in redox state and/or pH, antisecretory factor can exist in several conformational variants of antisecretory factor/PSMD4/S5a in porcine cerebrospinal fluid, which could be of functional importance.
the neuroprotective dose of isatin used in this study can result in brain isatin concentrations that are proapoptotic for cells in vitro, the altered repertoire of mitochondrial Rpn10-binding proteins may thus represent a part of a switch mechanism from targeted elimination of individual (damaged) proteins to more efficient ("global") elimination of damaged organelles and whole damaged cells.
this study showed that Rpn13 plays a redundant role with Rpn10 in recognition and degradation of ubiquitinated proteins in mouse livers.
Results demonstrate that Rpn10-mediated degradation of ubiquitinated proteins, catalyzed by ubiquitin-interacting motifs, is indispensable for mammalian life.
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core 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. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase 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 one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21.
proteasome (prosome, macropain) 26S subunit, non-ATPase, 4
, anti-secretory factor
, 26S proteasome non-ATPase regulatory subunit 4
, 26S proteasome subunit
, 26S proteasome regulatory subunit S5A
, type A von Willebrand factor domain-containing protein
, ubiquitin interacting motif domain-containing protein
, proteasome 26S subunit, non-ATPase, 4
, RPN10 homolog
, S5a/antisecretory factor protein
, antisecretory factor 1
, multiubiquitin chain-binding protein
, proteasome 26S subunit non-ATPase 4
, 26S proteasome regulatory subunit RPN10
, proteasome 26S non-ATPase subunit 4
, anti secretory factor 1
, multiubiquitin-chain-binding protein
, antisecretory factor