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anti-Human PSMD2 Antibodies:
anti-Mouse (Murine) PSMD2 Antibodies:
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Human Polyclonal PSMD2 Primary Antibody for ELISA, ICC - ABIN250329
Di Domenico, Coccia, Cocciolo, Murphy, Cenini, Head, Butterfield, Giorgi, Schinina, Mancuso, Cini, Perluigi: Impairment of proteostasis network in Down syndrome prior to the development of Alzheimer's disease neuropathology: redox proteomics analysis of human brain. in Biochimica et biophysica acta 2013
Show all 3 Pubmed References
Human Polyclonal PSMD2 Primary Antibody for ELISA, WB - ABIN547373
Kuai, Wooters, Hall, Rao, Nickbarg, Li, Chatterjee-Kishore, Qiu, Lin: NAK is recruited to the TNFR1 complex in a TNFalpha-dependent manner and mediates the production of RANTES: identification of endogenous TNFR-interacting proteins by a proteomic approach. in The Journal of biological chemistry 2004
Study found that PSMD2 was markedly upregulated in breast cancer. High PSMD2 expression was significantly correlated with poor prognosis. PSMD2 knockdown inhibited cell proliferation and arrested cell cycle at G0/G1 phase in vitro, as well as suppressed tumor growth in vivo. Mechanically, PSMD2 physically interacted with p21 and p27 and mediated their ubiquitin-proteasome degradation with the cooperation of USP14.
By recruiting the 26S proteasome and the ubiquitin-selective ATPase p97 to arsenite-induced stress granules, ZFAND1 ensures their timely clearance and prevents their aberration.
the high-resolution solution structure of the UBL domain of human UBLCP1 and its interaction with Rpn1
Results suggest that PSMD2 may be a good molecular target candidate.
These data suggest that p97 recruits proteasomes to polytopic ER proteins, such as Insig-1, even before they are extracted from membranes.
U87 glioblastoma cells transduced to express the epidermal growth factor receptor vIII (EGFRvIII) mutant do not respond toirrradiation with 26s proteasome inhibition.
Data show that data provide a novel mechanism whereby CaMKII may regulate the proteasome in neurons to facilitate remodeling of synaptic connections through protein degradation.
the 26S proteasome may provide a general predictive biomarker for radiotherapy outcome.
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. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1.
26S proteasome regulatory subunit S2
, 26S proteasome non-ATPase regulatory subunit 2
, 26s proteasome regulatory subunit S2-like protein
, proteasome (prosome, macropain) 26S subunit, non-ATPase, 2
, proteasome 26S non-ATPase subunit 2
, 55.11 protein
, TNFR-associated protein 2
, protein 55.11
, tumor necrosis factor type 1 receptor-associated protein 2
, 26S proteasome regulatory subunit RPN1
, 26S proteasome subunit p97
, testis expressed gene 190