Canine 20S Immunoproteasome Protein, CF
Canine 20S Immunoproteasome Protein, CF Summary
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, 1mM 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 multi-complex Immunoproteasome. The structure of the 20S Immunoproteasome is similar to the 20S Proteasome, which is composed of 28 non-identical subunits arranged into four stacked rings (1,2). However, during 20S Immunoproteasome assembly, the three catalytic beta subunits, beta 1, 2, and 5, in the two interior rings of the 20S Proteasome are replaced by three IFN-gamma-inducible catalytic subunits: beta 1i/LMP2, beta 2i/LMP7, and beta 5i/MECL-1 (3). The 20S Immunoproteasome is commonly associated with the 19S, PA28 alpha/beta, or the PA28 gamma regulatory complexes (3,4). 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 (3,5,6). Selective inhibition of 20S Immunoproteasome proteolytic activity using small molecule inhibitors is being examined for therapeutic intervention in cancer and inflammatory diseases (7).
This protein has been purified from canine spleen.
- Kim, H.M. et al. (2011) Biochim. Biophys. Acta 1809:67.
- Xie, Y. (2010) J. Mol. Cell Biol. 2:308.
- Kloetzel, P.M. (2001) Nat. Rev. Mol. Cell Biol. 2:179.
- Stadtmueller, B.M. & C.P. Hill (2011) Mol. Cell 41:8.
- Cascio, P. et al. (2001) EMBO J. 20:2357.
- Ferrington, D.A. & D.S. Gregerson (2012) Prog. Mol. Biol. Transl. Sci. 109:75.
- Lee, W. & K.B. Kim (2011) Curr. Top. Med. Chem. 11:2923.
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