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Human 20S Proteasome Protein, CF

Bio-Techne includes R&D Systems | Catalog # E-360

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E-360-050

Key Product Details

Source

Human Erythrocytes

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

Human erythrocyte-derived 20S Proteasome protein
The Human 20S Proteasome protein has been purified from human erythrocytes, which have been screened and are negative for hepatitis B surface antigen, antibodies to hepatitis C virus, HIV type 1 antigens, and antibodies to HIV type 1 and 2.

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Predicted Molecular Mass

700 kDa

Activity

The Human 20S Proteasome is able to degrade substrates in an ATP-independent manner. Reaction conditions will need to be optimized for each specific application. We recommend an initial Human 20S Proteasome concentration of 0.5-5 nM.

Formulation, Preparation and Storage

E-360
Formulation Supplied as a 0.2 μm filtered solution in HEPES, NaCl and DTT.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: 20S Proteasome

The 20S Proteasome is the catalytic core component of the multi-complex 26S Proteasome that selectively degrades intracellular proteins.  It is commonly associated with regulatory complexes, which include the 19S Proteasome, the PA28 alpha/beta complex, or the PA28 gamma complex (1). The 20S Proteasome is composed of 28 subunits arranged into four stacked rings (2,3). The outer rings, containing seven subunits each, are composed of closely-related but non-identical alpha subunits.  The amino-terminal tails of the alpha subunits form a gate that restricts substrate entry into the catalytic core.  The inner rings, also containing seven subunits each, are composed of closely-related but non-identical beta subunits.  The amino-terminal tails of six of the beta subunits, three per ring, have proteolytic activity. Inhibition of 20S Proteasome proteolytic core activity using small molecule inhibitors is a valuable tool for the functional study of a variety of proteins and for therapeutic intervention (4). The 20S Proteasome can be activated chemically by the addition of detergent or by the proteinaceous activator PA28 Activator alpha (5). 

The Human 20S Proteasome protein has been purified from human erythrocytes, which have been screened and are negative for hepatitis B surface antigen, antibodies to hepatitis C virus, HIV type 1 antigens, and antibodies to HIV type 1 and 2.

References

  1. Stadtmueller, B.M. & C.P. Hill (2011) Mol. Cell 41:8.
  2. Kim, H.M. et al. (2011) Biochim. Biophys. Acta 1809:67.
  3. Xie, Y. (2010) J. Mol. Cell Biol. 2:308.
  4. Kisselev, A.F. et al. (2012) Chem. Biol. 19:99.
  5. Ma, C.P. et al. (1992) J. Biol. Chem. 267:10515.

Additional 20S Proteasome Products

Product Documents for Human 20S Proteasome Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Human 20S Proteasome Protein, CF

For research use only

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