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Boston Biochem/Human 20S Proteasome Protein, CF/E-360-050

价格
¥4020.00
货号:E-360-050
浏览量:64
品牌:Boston Biochem
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Citations (21)
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SummaryProduct DatasheetsCarrier FreeReconstitution CalculatorBackgroundRelated Research Areas

Human 20S Proteasome Protein, CF Summary

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Activity
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
Predicted Molecular Mass
700 kDa

Product Datasheets

Product Datasheet
COA

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

E-360

Formulation

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

ShippingThe 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.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: 20S Proteasome

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.

References
  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.
Alternate Names
20S Proteasome

Citations for Human 20S Proteasome Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products.The data collected includes not only links to publications in PubMed,but also provides information about sample types, species, and experimental conditions.

21Citations: Showing 1 - 10Filter your results:

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  1. A dual inhibitor of the proteasome catalytic subunits LMP2 and Y attenuates disease progression in mouse models of Alzheimer's diseaseAuthors: IJ Yeo, MJ Lee, A Baek, Z Miller, D Bhattarai, YM Baek, HJ Jeong, YK Kim, DE Kim, JT Hong, KB KimSci Rep, 2019;9(1):18393.Species: MouseSample Types: Tissue Culture SupernatesApplications: Bioassay
  2. Discovery of Immunoproteasome Inhibitors Using Large-Scale Covalent Virtual ScreeningAuthors: A Scarpino, D Bajusz, M Proj, M Gobec, I Sosi?, S Gobec, GG Ferenczy, GM Keser?Molecules, 2019;24(14):.Species: HumanSample Types: Covalent CompoundsApplications: Bioassay
  3. REG? controls Hippo signaling and reciprocal NF-?B-YAP regulation to promote colon cancerAuthors: 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 DangClin. Cancer Res., 2018;0(0):.Species: HumanSample Types: Recombinant ProteinApplications: Bioassay
  4. Piperlongumine and some of its analogs inhibit selectively the human immunoproteasome over the constitutive proteasomeAuthors: E Bosc, J Nastri, V Lefort, M Valli, F Contiguiba, R Pioli, M Furlan, VDS Bolzani, C El Amri, M Reboud-RavBiochem. Biophys. Res. Commun., 2018;496(3):961-966.Species: HumanSample Types: Small MoleculeApplications: Bioassay
  5. A new gold(I) complex-Au(PPh3)PT is a deubiquitinase inhibitor and inhibits tumor growthAuthors: X Li, Q Huang, H Long, P Zhang, H Su, J LiuEBioMedicine, 2018;0(0):.Species: HumanSample Types: Recombinant ProteinApplications: Bioassay
  6. Diabetogenic agent alloxan is a proteasome inhibitorAuthors: W Zhou, L Wei, T Xiao, C Lai, M Peng, L Xu, X Luo, S Deng, F ZhangBiochem. Biophys. Res. Commun., 2017;0(0):.Applications: Bioassay
  7. A therapeutic T cell receptor mimic antibody targets tumor-associated PRAME peptide/HLA-I antigensAuthors: 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 ScheinbergJ. Clin. Invest., 2017;127(7):2705-2718.Species: N/ASample Types: ProteinApplications: Enzyme Assay
  8. Immunohistochemical analysis reveals variations in proteasome tissue expression in C. elegansAuthors: E Mikkonen, C Haglund, CI HolmbergPLoS ONE, 2017;12(8):e0183403.Species: C. elegansSample Types: Whole TissueApplications: IHC-P
  9. Immunoproteasome functions explained by divergence in cleavage specificity and regulationAuthors: 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 CraikElife, 2017;6(0):.Species: HumanSample Types: Recombinant ProteinApplications: Bioassay
  10. Clinical activity of carfilzomib correlates with inhibition of multiple proteasome subunits: application of a novel pharmacodynamic assayAuthors: SJ Lee, K Levitsky, F Parlati, MK Bennett, S Arastu-Kap, L Kellerman, TF Woo, AF Wong, KP Papadopoul, R Niesvizky, AZ Badros, R Vij, S Jagannath, D Siegel, M Wang, GJ Ahmann, CJ KirkBr J Haematol, 2016;0(0):.Species: HumanSample Types: Cell LysatesApplications: Bioassay
  11. APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the ProteasomeInt J Mol Sci, 2016;17(10):.Species: HumanSample Types: ProteinApplications: Bioassay
  12. Copper(II) ions affect the gating dynamics of the 20S proteasome: a molecular and in cell studySci Rep, 2016;6(0):33444.Species: N/ASample Types: ProteinApplications: Bioassay
  13. Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease andIdentification of Novel Peptide Substrates and Boronate Inhibitors withAnti-bacterial Activity.Authors: Akopian T, Kandror O, Tsu C, Lai J, Wu W, Liu Y, Zhao P, Park A, Wolf L, Dick L, Rubin E, Bachovchin W, Goldberg AJ Biol Chem, 2015;290(17):11008-20.Species: Bacteria - Mycobacterium tuberculosisSample Types: ProteinApplications: Bioassay
  14. Structure- and function-based design of Plasmodium-selective proteasomeinhibitors.Authors: Li H, O"Donoghue A, van der Linden W, Xie S, Yoo E, Foe I, Tilley L, Craik C, da Fonseca P, Bogyo MNature, 2015;530(7589):233-6.Species: HumanSample Types: ProteinApplications: Enzyme Assay
  15. VR23: A Quinoline-Sulfonyl Hybrid Proteasome Inhibitor That Selectively KillsCancer via Cyclin E-Mediated Centrosome Amplification.Authors: Pundir S, Vu H, Solomon V, McClure R, Lee HCancer Res, 2015;75(19):4164-75.Species: N/ASample Types: Peptide
  16. Nucleolar stress induces ubiquitination-independent proteasomal degradation of PICT1 protein.Authors: Maehama, Tomohiko, Kawahara, Kohichi, Nishio, Miki, Suzuki, Akira, Hanada, KentaroJ Biol Chem, 2014;289(30):20802-12.Species: HumanSample Types: ProteinApplications: Bioassay
  17. Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.Authors: Debowski D, Pikula M, Lubos M, Langa P, Trzonkowski P, Lesner A, Legowska A, Rolka KPLoS ONE, 2014;9(2):e89465.Species: N/ASample Types: ProteinApplications: Bioassay
  18. Gold(III)-dithiocarbamato peptidomimetics in the forefront of the targeted anticancer therapy: preclinical studies against human breast neoplasia.Authors: Nardon, Chiara, Schmitt, Sara M, Yang, Huanjie, Zuo, Jian, Fregona, Dolores, Dou, Q PingPLoS ONE, 2014;9(1):e84248.Species: HumanSample Types: Cell Extracts
  19. RedOx status, proteasome and APEH: insights into anticancer mechanisms oft10,c12-conjugated linoleic acid isomer on A375 melanoma cells.Authors: Bergamo P, Cocca E, Palumbo R, Gogliettino M, Rossi M, Palmieri GPLoS ONE, 2013;8(11):e80900.
  20. Enzymatic discovery of a HER-2/neu epitope that generates cross-reactive T cells.Authors: Henle A, Erskine C, Benson L, Clynes R, Knutson KJ Immunol, 2013;190(1):479-88.Species: N/ASample Types: Recombinant ProteinApplications: Bioassay
  21. Selective cytotoxicity of amidinopiperidine based compounds towards Burkitt'slymphoma cells involves proteasome inhibition.Authors: Gobec M, Obreza A, Prijatelj M, Brus B, Gobec S, Mlinaric-Rascan IPLoS ONE, 2012;7(7):e41961.Species: HumanSample Types: ProteinApplications: Bioassay

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