Background:  In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S Proteasome. The 26S Proteasome is a protease complex that selectively breaks down proteins that have been modified by polyubiquitin chains. It is made up of two multisubunit complexes: the 20S Proteasome chamber, which serves as the proteolytic core of the complex and two 19S regulatory particles which recognize and unfold ubiquitinated proteins. PSMD7 (proteasome (prosome, macropain) 26S subunit, non-ATPase 7), also referred to as P40, S12 or MOV34, is a regulatory subunit of the 26S Proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. PSMD7 contains a proteolytically resistant MPN domain. MPN domain family members comprise subunits of the proteasome, COP9-signalosome and eIF3 (translation initiation factor 3) complexes. PSMD7 interacts with HIV-1 Vpr and together they function as a cellular factor linked to the G2/M phase transition of the mammalian cell cycle.

Description: Rabbit polyclonal to PSMD7

Immunogen: KLH conjugated synthetic peptide derived from PSMD7

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 37 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.