20S Proteasome α7 Antibody (MCP72): sc-58417

20S Proteasome α7 Antibody (MCP72) is a mouse monoclonal IgG1 antibody that detects 20S Proteasome α7 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-20S Proteasome α7 antibody (MCP72) is available in a non-conjugated form, specifically designed for researchers studying the proteasome′s critical role in cellular protein regulation. The 20S proteasome is a vital component of the ubiquitin-proteasome system, responsible for degrading misfolded, damaged, or unneeded proteins, maintaining cellular homeostasis and regulating various cellular processes, including cell cycle and apoptosis. The structure of the 20S proteasome core consists of a cylindrical arrangement of 28 subunits, forming a hollow chamber where proteolysis occurs. This unique architecture allows for selective entry of substrates while preventing uncontrolled degradation, ensuring that only proteins tagged for destruction are processed. The outer rings of the core are composed of α subunits that serve as gates, while the inner rings contain β subunits that possess catalytic activity, highlighting the intricate design that underpins the proteasome′s function in cellular proteostasis.

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20S Proteasome α7 Antibody (MCP72) References:

1. Primary structural features of the 20S proteasome subunits of rice (Oryza sativa).  |  Sassa, H., et al. 2000. Gene. 250: 61-6. PMID: 10854779
2. Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.  |  Ferrington, DA. and Kapphahn, RJ. 2004. FEBS Lett. 578: 217-23. PMID: 15589823
3. Optimization of subsite binding to the beta5 subunit of the human 20S proteasome using vinyl sulfones and 2-keto-1,3,4-oxadiazoles: syntheses and cellular properties of potent, selective proteasome inhibitors.  |  Rydzewski, RM., et al. 2006. J Med Chem. 49: 2953-68. PMID: 16686537
4. Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6.  |  Ishii, K., et al. 2015. Sci Rep. 5: 18167. PMID: 26657688
5. Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy.  |  Kozai, T., et al. 2017. Sci Rep. 7: 15373. PMID: 29133893
6. Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism.  |  Song, C., et al. 2021. Int J Mol Sci. 22: PMID: 33926037
7. Ordered structure of the crystallized bovine 20S proteasome.  |  Morimoto, Y., et al. 1995. J Biochem. 117: 471-4. PMID: 7629009
8. Conformational constraints in protein degradation by the 20S proteasome.  |  Wenzel, T. and Baumeister, W. 1995. Nat Struct Biol. 2: 199-204. PMID: 7773788
9. Structure and structure formation of the 20S proteasome.  |  Schmidt, M., et al. 1997. Mol Biol Rep. 24: 103-12. PMID: 9228290
10. Human proteasome subunits from 2-dimensional gels identified by partial sequencing.  |  Kristensen, P., et al. 1994. Biochem Biophys Res Commun. 205: 1785-9. PMID: 7811265
11. Comprehensive mass spectrometric analysis of the 20S proteasome complex.  |  Huang, L. and Burlingame, AL. 2005. Methods Enzymol. 405: 187-236. PMID: 16413316
12. Role of the beta1 subunit in the function and stability of the 20S proteasome in the hyperthermophilic archaeon Pyrococcus furiosus.  |  Madding, LS., et al. 2007. J Bacteriol. 189: 583-90. PMID: 17114253

The preferred 20S Proteasome α7/α8 antibody is 20S Proteasome α7/α8 Antibody (B-4): sc-166761.