Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

antibody

Proteasome 19S Rpt4/S10b subunit polyclonal antibody

BML-PW8220-0025

25 µl

polyclonal

domestic rabbit

nonconjugated

western blot, immunohistochemistry

BML-PW8220-0025

Proteasome 19S Rpt4/S10b subunit polyclonal antibody

Rabbit

Polyclonal

Antibody

25 µl

Human, Yeast

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 sub-unit 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 ubstrate prior to insertion into the proteolytic core of the 20S proteasomes.

Proteasome subunit p42, 26S protease regulatory subunit 10B, Proteasome 26S subunit ATPase 6

Recombinant full length human p42.

Recognizes the Rpt4/S10b subunit of the 19S regulator complex.

Liquid. In PBS containing 10mM sodium azide.

Detects a band of ~44kDa by Western blot.

IHC, WB

-20°C