Human Ramos Cell 20S Immunoproteasome Protein, CF
Human Ramos Cell 20S Immunoproteasome Protein, CF Summary
The human 20S Immunoproteasome is able to degrade substrates in an ATP-independent manner in vitro. It can be activated chemically with SDS (0.035%) or by the addition of PA28. Reaction conditions will need to be optimized for each specific application. We recommend an initial i20S Proteasome concentration of 0.5-5 nM.
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
X mg/ml (X μM) in 50 mM HEPES pH 7.6, 100 mM NaCl, 1 mM 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.
Background: 20S Immunoproteasome
The 20S Immunoproteasome is a modified form of the constitutively active 20S Proteasome core particle and is the catalytic subunit of the multicomplex Immunoproteasome. The structure of the 20S Immunoproteasome is similar to the 20S Proteasome, which is composed of 28 nonidentical subunits arranged into four stacked rings. However, during 20S Immunoproteasome assembly, the three catalytic beta subunits, beta 1, beta 2, and beta 5, in the two interior rings of the 20S Proteasome are replaced by three IFN gamma -inducible catalytic subunits: beta 1i/LMP2, beta 2i/MECl1, and beta 5i/LMP7. The 20S Immunoproteasome is commonly associated with the 19S, PA28 alpha / beta, or the PA28 gamma regulatory complexes. 20S Immunoproteasome expression is enriched in antigen presenting cells of the immune system where the 20S Immunoproteasome selectively degrades intracellular proteins in a manner that optimizes the generation of peptides for MHC class I antigen presentation. Selective inhibition of 20S Immunoproteasome proteolytic activity using small molecule inhibitors is being examined for therapeutic intervention in cancer and inflammatory diseases. This protein complex has been purified from Burkitt's lymphoma cells (Ramos, RA1, CRL-1596) following stimulation with IFN-gamma and IL-2.
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