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High PSMA3 expression is associated with cholangiocarcinoma.
In thyroid hemiagenesis, genomic examinations revealed the presence of four recurrent defects (three deletions and one duplication) affecting highly conservative proteasome genes PSMA1, PSMA3, and PSMD3.
Our results provide evidence on new T1DM-susceptible loci in the PSMA3, PSMA6 and PSMC6 proteasome genes and give a new insight into the T1DM pathogenesis
Evidence of a sex-specific association of PSMA3 genetic variants with subtypes of juvenile idiopathic arthritis.
Protein interaction between Ambn and Psma3 can facilitate redistribution of ameloblastin domains within forming enamel.
A combination of two-dimensional gel electrophoresis (2D-GE) and tandem mass-spectrometry revealed a large number of PSMA3-bound proteins that are involved in various aspects of mRNA metabolism, including splicing.
Serum 20S proteasome concentration and percentage of lymphocytic apoptosis predicted survival and patient prognosis in critically ill patients.
Plasminogen activator inhibitor type 1 interacts with alpha3 subunit of proteasome and modulates its activity.
Aurora-B might undergo degradation by binding to HC8 in a proteasome-dependent manner during mitosis
EBNA3C binds to human the C8/alpha7 subunit of the 20S proteasome; degraded by purified 20S proteasomes in vitro but, found to be very stable and apparently turned over at a very low rate in B cells infected latently with EBV
The authors propose that the full-length HCV F protein as well as the F protein initiating from codon 26 is degraded by an ubiquitin-independent pathway that is mediated by the proteasome subunit alpha3.
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 peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified.
macropain subunit C8
, multicatalytic endopeptidase complex subunit C8
, proteasome component C8
, proteasome subunit C8
, proteasome subunit alpha type-3
, multicatalytic proteinase subunit K
, proteasome subunit K
, proteasome (prosome, macropain) subunit, alpha type, 3
, molybdenum cofactor sulfurase
, proteasome alpha 3 subunit