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20S Immunoproteasome
(Untagged, Purified from the human spleen)
50 μg - price inquire

Immuno20S figure.png
SDS-PAGE i20S Nov2024_1.png

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20S immunoproteasome purified from human spleen. Human 20S immunoproteasomes were separated from standard 20S to apparent homogeneity. (A) Chromatogram depicting the separation. (B) Immunoblotting of 20S immunoproteasome (LMPT-7) and standard 20S (MB1). (C) Coomassie stained 12% SDS-PAGE following a final column purification step. A clear separation between immunoproteasome 20S and standard 20S purified from human spleen is achieved. 

Product Details

Source: Purified from the human spleen by fractionation. Exhibits the highest activity, soluble and homogenous. All starting material has been tested and found to be negative for hepatitis B surface antigen, human immunodeficiency virus type 1 antigen, antibodies against human immunodeficiency viruses type 1 and 2, and hepatitis C virus.
Formulation: Liquid. In 20mM Tris-HCl, 1mM sodium azide, 1mM DTT, pH 7.2. Contains 50% glycerol.

Buffer ingredients can be adjusted to customer needs.
Shipping: Shipped on Dry Ice
Long Term Storage: -80°C. Avoid freeze/thaw cycles.

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Scientific Background

The eukaryotic proteasome contains 7α-type and 7 β-type subunits. Upon stimulation with IFN-γ, the three active β subunits, β1 (Y), β2 (Z) and β5 (X) are exchanged to their immunocounterparts, namely β1i (LMP-2), β2i (MECL-1) and β5i (LMP-7). This results in a change in proteasomal substrate specificity. Some groups have reported increases in chymotrypsin-like and trypsin-like activities while others have reported no changes or even decreased activities after such treatment.​

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Product Literature References
1) Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks, Jean Lesne and Julien Marcoux et al.; Nat Commun.,11: 6140, (2020), Full Text

 

2) Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in α-Synuclein Aggregation Disorders, Scott Ugras and Harry Ischiropoulos et al.; EBioMedicine., 31: 307–319, (2018), Full Text

 

3) The presence of prolines in the flanking region of an immunodominant HIV‐2 gag epitope influences the quality and quantity of the epitope generated, Sabelle Jallow and Sarah L. Rowland‐Jones et al.; Eur J Immunol., 45(8): 2232–2242, (2015), Full Text

 

4) Differential Roles of Proteasome and Immunoproteasome Regulators Pa28αβ, Pa28γ and Pa200 in the Degradation of Oxidized Proteins, Andrew. M. Pickering and Kelvin. J. A. Davies; Arch Biochem Biophys., 523(2): 181–190, (2012), Full Text

 

5) Pivotal Advance: Protein synthesis modulates responsiveness of differentiating and malignant plasma cells to proteasome inhibitors, Simone Cenci and Paolo Cascio et al. J Leukoc Biol., 92(5):921-31, (2012), Full Text

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