Product Details
| Source: | Isolated from human spleen. |
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| Formulation: | Liquid. In TEAD buffer (20mM TRIS/HCl, 1mM sodium azide, 1mM DTT, pH 7.4). Contains 50% glycerol. |
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| Purity Detail: | Highly purified. All starting material has been tested and found to be negative for hepatitis B surface antigen, human immunodeficiency virus type 1 antigens, and antibodies against human immunodeficiency viruses type 1 and 2, and hepatitis C virus. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Once thawed the material can be stored at +4°C for up to 3 months, or long term at -20°C. |
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| Handling: | 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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| Regulatory Status: | RUO - Research Use Only |
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Western blot analysis of Immunoproteasome 20S (human), (purified) (Prod. No. BML-PW9645) probed with anti-Syntaxin 3 antibody (ab4113) and anti-Proteasome 20S LMP2 antibody (ab42987).
Coomassie stained gel after SDS-PAGE (12.5% acrylamide). Lane (a): molecular weight markers; lane (b) 20S immunoproteosome, spleen-derived (prod.no. BML-PW9645); lane (c): 20S proteosome, erythrocyte-derived (PW8720).
All activities were measured by use of 200µM substrate concentration (final concentration) all dissolved in TEAD buffer. Test system: 20µl enzyme solution (640ng); 20µl substrate solution (incubation at 37°C); 200µl stop solution (100mM sodium chloroacetate dissolved in 30mM Na-acetate, 70mM acetic acid, pH 4.3). Fluorescence was measured in a microplate fluorimeter at 355nm excitation and 460nm emission.
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Product Literature References
Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks: J. Lesne, et al.; Nat. Commun.
11, 6140 (2021),
Abstract;
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Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in α-Synuclein Aggregation Disorders: S. Ugras, et al.; EBioMedicine
31, 307 (2018),
Abstract;
Full Text
The presence of prolines in the flanking region of an immunodominant HIV-2 gag epitope influences the quality and quantity of the epitope generated: S. Jallow, et al.; Eur. J. Immunol.
45, 2232 (2015),
Abstract;
Full Text
Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins: A.M. Pickering, et al.; Arch. Biochem. Biophys.
523, 181 (2012),
Abstract;
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Pivotal advance: protein synthesis modulates responsiveness of differentiating and malignant plasma cells to proteasome inhibitors: S. Cenci, et al.; J. Leukoc. Biol.
92, 921 (2012),
Abstract;
