PSMD7 Protein, proteasome (prosome, macropain) 26S subunit, non-ATPase, 7

PSMD7

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PSMD7

Official Full Name proteasome (prosome, macropain) 26S subunit, non-ATPase, 7
Background 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 a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17.
Synonyms PSMD7; proteasome (prosome, macropain) 26S subunit, non-ATPase, 7; proteasome (prosome, macropain) 26S subunit, non ATPase, 7 (Mov34 homolog); 26S proteasome non-ATPase regulatory subunit 7; MOV34; Mov34 homolog; P40; Rpn8; S12; proteasome subunit p40; 26S proteasome regulatory subunit S12; 26S proteasome regulatory subunit rpn8; Moloney leukemia virus-34 proviral integration; proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)
    • Species :
    • Human
    • Rhesus Macaque
    • Zebrafish
    • Source :
    • E.coli
    • HEK293
    • Mammalian Cell
    • Tag :
    • GST
    • His
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human PSMD7-2032H Recombinant Human PSMD7, GST-tagged E.coli GST
    Human PSMD7-2745HCL Recombinant Human PSMD7 293 Cell Lysate HEK293 N/A
    Human PSMD7-31228TH Recombinant Human PSMD7, His-tagged E.coli His
    Human PSMD7-424H Recombinant Human PSMD7 Protein, His-tagged E.coli His
    Rhesus Macaque PSMD7-3674R Recombinant Rhesus monkey PSMD7 Protein, His-tagged Mammalian Cell His
    Zebrafish PSMD7-10177Z Recombinant Zebrafish PSMD7 Mammalian Cell His

    PSMD7 involved in several pathways and played different roles in them. We selected most pathways PSMD7 participated on our site, such as Proteasome, Epstein-Barr virus infection, which may be useful for your reference. Also, other proteins which involved in the same pathway with PSMD7 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Proteasome PSMD4; PSMA1; PSMB9B; PSME4; PSMD11; PSMC4; POMP; PSMC6; PSMB9A; PSMC2
    Epstein-Barr virus infection TRAF3; HDAC4; MAPK10; PSMC1; PSMC2; TBPL1; POLR2K; HDAC5; PIK3R5; PLCG2

    PSMD7 has several biochemical functions, for example, protein binding, protein homodimerization activity. Some of the functions are cooperated with other proteins, some of the functions could acted by PSMD7 itself. We selected most functions PSMD7 had, and list some proteins which have the same functions with PSMD7. You can find most of the proteins on our site.

    Function Related Protein
    protein binding FLII; HERPUD1; TFRC; SRC; FAM134B; STAT3; SOX6; SF3B3; TNFSF13B; CDK18
    protein homodimerization activity MZF1; G6PD; DNTTIP1; PDXK; XCL1; MAFA; UBE4A; MLL1; MBL1; DCK

    PSMD7 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PSMD7 here. Most of them are supplied by our site. Hope this information will be useful for your research of PSMD7.

    PSMD14; UCHL5; PSMD10; PSMC4; PSMC6; PSMD6; TRAF6

    Pathare, GR; Nagy, I; et al. Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 111:2984-2989(2014).
    Huang, SP; Lin, VC; et al. Genetic variants in nuclear factor-kappa B binding sites are associated with clinical outcomes in prostate cancer patients. EUROPEAN JOURNAL OF CANCER 49:3729-3737(2013).

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