Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

antibody

Proteasome 19S ATPase subunit Rpt6/S8 (human) polyclonal antibody

BML-PW8320-0025

25 µl

polyclonal

domestic rabbit

nonconjugated

BML-PW8320-0025

Proteasome 19S ATPase subunit Rpt6/S8 (human) polyclonal antibody

Rabbit

Polyclonal

Antibody

25 µl

Human

The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. In addition to the 20S particle, the 26S complex contains over twenty additional proteins, ranging in molecular weight from 25 to 10kDa, located in a distinct complex called the 'PA700 proteasome activator' or the '19S complex', and which determines substrate specificity and provides the multiple enzymatic functions necessary for proteolysis and viability. Systematic analysis of the subunit components have revealed at least six members to be ATPases belonging to a new family of ATP-binding proteins, together with a further fifteen sub-units that lack the capacity to bind ATP, isopeptidases and several other proteins thought to be responsible for the unfolding of a protein substrate prior to insertion into the proteolytic core of the 20S proteasome.

TRIP1, 26S protease regulatory subunit 5, Proteasome 26S subunit ATPase 5, Thyroid hormone receptor-interacting protein 1, p45/SUG

Recombinant full length human His6-FLAG-tagged Rpt6

Recognizes the Rpt6/S8 subunit of the 19S regulator complex.

Liquid. In PBS containing 10mM sodium azide.

Single dimension SDS-PAGE of a human placental proteasome preparation followed by Western blotting gives a single band with a relative molecular weight of approximately 48kDa. The antibody reacts strongly with the recombinant protein and immunoreactivity is abolished upon preincubation of the antibody with recombinant protein. The antibody clearly detects the presence of the desired protein in HeLa cell lysates although other bands of higher molecular weight are observed the nature of which are unknown.

WB

-20°C