Human 20S Proteasome Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Human 20S Proteasome Protein, CF Summary

Details of Functionality
The Human 20S Proteasome is able to degrade substrates in an ATP-independent manner. 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 Human 20S Proteasome concentration of 0.5-5 nM.
Source
Human erythrocyte-derived 20S Proteasome protein
Protein/Peptide Type
Natural Enzymes
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

Theoretical MW
700 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
E-360 in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer

X mg/ml (X μM) in 50 mM HEPES pH 7.6, 100 mM NaCl, 1 mM DTT

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Human 20S Proteasome Protein, CF

  • 20S Proteasome

Background

The 20S Proteasome is the catalytic core component of the multi-complex 26S Proteasome that selectively degrades intracellular proteins.  It is commonly associated with regulatory complexes, which include the 19S Proteasome, the PA28 alpha/beta complex, or the PA28 gamma complex (1). The 20S Proteasome is composed of 28 subunits arranged into four stacked rings (2,3). The outer rings, containing seven subunits each, are composed of closely-related but non-identical alpha subunits.  The amino-terminal tails of the alpha subunits form a gate that restricts substrate entry into the catalytic core.  The inner rings, also containing seven subunits each, are composed of closely-related but non-identical beta subunits.  The amino-terminal tails of six of the beta subunits, three per ring, have proteolytic activity. Inhibition of 20S Proteasome proteolytic core activity using small molecule inhibitors is a valuable tool for the functional study of a variety of proteins and for therapeutic intervention (4). The 20S Proteasome can be activated chemically by the addition of detergent or by the proteinaceous activator PA28 Activator alpha (5). 

The Human 20S Proteasome protein has been purified from human erythrocytes, which have been screened and are negative for hepatitis B surface antigen, antibodies to hepatitis C virus, HIV type 1 antigens, and antibodies to HIV type 1 and 2.

  1. Stadtmueller, B.M. & C.P. Hill (2011) Mol. Cell 41:8.
  2. Kim, H.M. et al. (2011) Biochim. Biophys. Acta 1809:67.
  3. Xie, Y. (2010) J. Mol. Cell Biol. 2:308.
  4. Kisselev, A.F. et al. (2012) Chem. Biol. 19:99.
  5. Ma, C.P. et al. (1992) J. Biol. Chem. 267:10515.

Publications for 20S Proteasome (E-360)(21)

We have publications tested in 5 confirmed species: Human, Mouse, Bacteria - Mycobacterium tuberculosis, C. elegans, N/A.

We have publications tested in 3 applications: Bioassay, Enzyme Assay, IHC-P.


Filter By Application
Bioassay
(15)
Enzyme Assay
(2)
IHC-P
(1)
All Applications
Filter By Species
Human
(11)
Mouse
(1)
Bacteria - Mycobacterium tuberculosis
(1)
C. elegans
(1)
N/A
(5)
All Species
Showing Publications 1 - 10 of 21. Show All 21 Publications.
Publications using E-360 Applications Species
IJ Yeo, MJ Lee, A Baek, Z Miller, D Bhattarai, YM Baek, HJ Jeong, YK Kim, DE Kim, JT Hong, KB Kim A dual inhibitor of the proteasome catalytic subunits LMP2 and Y attenuates disease progression in mouse models of Alzheimer's disease Sci Rep, 2019;9(1):18393. 2019 [PMID: 31804556] (Bioassay, Mouse) Bioassay Mouse
A Scarpino, D Bajusz, M Proj, M Gobec, I Sosi?, S Gobec, GG Ferenczy, GM Keser? Discovery of Immunoproteasome Inhibitors Using Large-Scale Covalent Virtual Screening Molecules, 2019;24(14):. 2019 [PMID: 31315311] (Bioassay, Human) Bioassay Human
X Li, Q Huang, H Long, P Zhang, H Su, J Liu A new gold(I) complex-Au(PPh3)PT is a deubiquitinase inhibitor and inhibits tumor growth EBioMedicine, 2018;0(0):. 2018 [PMID: 30527624] (Bioassay, Human) Bioassay Human
X Li, Q Wang, X Gao, T Yu, L Yuan, J Dai, W Wang, G Chen, C Jiao, W Zhou, Q Huang, L Cui, P Zhang, RE Moses, J Yang, F Chen, J Fu, J Xiao, L Li, Y Dang REG? controls Hippo signaling and reciprocal NF-?B-YAP regulation to promote colon cancer Clin. Cancer Res., 2018;0(0):. 2018 [PMID: 29437787] (Bioassay, Human) Bioassay Human
E Bosc, J Nastri, V Lefort, M Valli, F Contiguiba, R Pioli, M Furlan, VDS Bolzani, C El Amri, M Reboud-Rav Piperlongumine and some of its analogs inhibit selectively the human immunoproteasome over the constitutive proteasome Biochem. Biophys. Res. Commun., 2018;496(3):961-966. 2018 [PMID: 29355526] (Bioassay, Human) Bioassay Human
MB Winter, F La Greca, S Arastu-Kap, F Caiazza, P Cimermanci, TJ Buchholz, JL Anderl, M Ravalin, MF Bohn, A Sali, AJ O'Donoghue, CS Craik Immunoproteasome functions explained by divergence in cleavage specificity and regulation Elife, 2017;6(0):. 2017 [PMID: 29182146] (Bioassay, Human) Bioassay Human
E Mikkonen, C Haglund, CI Holmberg Immunohistochemical analysis reveals variations in proteasome tissue expression in C. elegans PLoS ONE, 2017;12(8):e0183403. 2017 [PMID: 28817671] (IHC-P, C. elegans) IHC-P C. elegans
AY Chang, T Dao, RS Gejman, CA Jarvis, A Scott, L Dubrovsky, MD Mathias, T Korontsvit, V Zakhaleva, M Curcio, RC Hendrickso, C Liu, DA Scheinberg A therapeutic T cell receptor mimic antibody targets tumor-associated PRAME peptide/HLA-I antigens J. Clin. Invest., 2017;127(7):2705-2718. 2017 [PMID: 28628042] (Enzyme Assay, N/A) Enzyme Assay N/A
W Zhou, L Wei, T Xiao, C Lai, M Peng, L Xu, X Luo, S Deng, F Zhang Diabetogenic agent alloxan is a proteasome inhibitor Biochem. Biophys. Res. Commun., 2017;0(0):. 2017 [PMID: 28502636] (Bioassay) Bioassay
APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the Proteasome Int J Mol Sci, 2016;17(10):. 2016 [PMID: 27669226] (Bioassay, Human) Bioassay Human
Show All 21 Publications.

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