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Human 26S Proteasome Protein, CF

Catalog #: E-365
14 Citations Datasheet / COA / SDS

Discontinued Product

E-365 has been discontinued.
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Product Details
Citations (14)
FAQs
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Summary Product Datasheets Carrier Free Reconstitution Calculator Background Related Research Areas

Human 26S Proteasome Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Activity
The Human 26S Proteasome can be used for in vitro degradation of appropriate substrates. The Human 26S Proteasome should be used immediately after thawing since it is inherently labile and will dissociate into free 20S and 19S subcomplexes over time. Reaction conditions will need to be optimized for each specific application. We recommend an initial Human 26S Proteasome concentration of 2-20 nM.
Source
Human embryonic kidney cell, HEK293-derived 26S Proteasome protein
Predicted Molecular Mass
2,100 kDa

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E-365

Product Datasheet
COA
SDS

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-365

Formulation

X mg/ml (X μM) in 20 mM HEPES pH 7.5, 20 mM NaCl, 2 mM Mg-ATP, 15% (v/v) Glycerol
Shipping The 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: 26S Proteasome

The 26S Proteasome is the major non-lysosomal protease in eukaryotic cells and is responsible for the degradation of ubiquitinated substrates and misfolded proteins. It is composed of two subcomplexes: the 20S Proteasome core particle and the 19S Proteasome regulatory particle. The 20S Proteasome facilitates proteolytic cleavage of protein substrates and is composed of 28 subunits arranged into four stacked rings (1,2). The outer rings of the 20S Proteasome are composed of seven related but non-identical, non-catalytic subunits, alpha1-7, that form a gate and restrict substrate access. The inner rings of the 20S Proteasome are composed of seven related but non-identical subunits, beta1-7. Beta1, 2, and 5 have proteyolytic activity. The 19S Proteasome caps one or both ends of the core particle and regulates substrate access to the catalytic core in an ATP-dependent manner by modulating 20S Proteasome conformation (3-5). The 19S Proteasome consists of a base subcomplex and a lid subcomplex. The base subcomplex is composed of six AAA+ family members, scaffolding proteins, and regulatory proteins involved in Ubiquitin recognition (2,6). The 19S Proteasome lid subcomplex contains eight subunits plus one deubiquitinating enzyme, Rpn11 (2,6). Small molecules that inhibit the activity of the 26S Proteasome are used to study the function of short-lived intracellular proteins and for the clinical treatment of certain forms of cancer (7). This highly purified 26S Proteasome preparation (from the transformed HEK cell line) can be used in vitro for the degradation of peptide substrates and poly-ubiquitinated proteins.

References
  1. Kim, H.M. et al. (2011) Biochim. Biophys. Acta 1809:67.
  2. Xie, Y. (2010) J. Mol. Cell Biol. 2:308.
  3. Adams, G.M. et al. (1998) Biochemistry 37:12927.
  4. Chu-Ping, M. et al. (1994) J. Biol. Chem. 269:3539.
  5. Kohler, A. et al. (2001) Mol. Cell 7:1143.
  6. Stadtmueller, B.M. & C.P. Hill (2011) Mol. Cell 41:8.
  7. Kisselev, A.F. et al. (2012) Chem. Biol. 19:99.
  8. Bajorek M. and Glickman M.H. (2004) Cell. Mol. Life Sci. 61: 1579-15882.
  9. DeMartino G.N. and Slaughter C.A. (1999) J. Biol. Chem. 274: 22123-221263.
  10. Driscoll J. and Goldberg A.L. (1990) J. Biol. Chem. 265: 4789-47924.
  11. Ferrell K., et al. (2000) Tren.Bioch.Sci 25: 83-885.
  12. Ganoth D., et al. (1988) J. Biol. Chem. 263: 12412-124196.
  13. Glickman M.H. and Maytal V. (2002). Curr. Top. Microbio. Immun. 268: 430727.
  14. Hartmann-Peterson R., et al. (2003) Tren.Bioch.Sci 28: 26-318.
  15. Kisselev A.F. and Goldberg A.L. (2005) Meth. Enz. 398: 364-3789.
  16. Voges D., et al. (1999) Ann. Rev. Biochem. 68: 1015-106810.
  17. Wang X., et al. (2007) Biochem. 46: 3553-356311.
  18. Waxman L., et al. (1987) J. Biol. Chem. 262: 2451-2457.
Alternate Names
26S Proteasome

Citations for Human 26S 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.

14 Citations: Showing 1 - 10
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  1. Floxuridine supports UPS independent of germline signaling and proteostasis regulators via involvement of detoxification in C. elegans
    Authors: Dubey, AA;Sarkar, A;Milcz, K;Szulc, NA;Thapa, P;Piechota, M;Serwa, RA;Pokrzywa, W;
    PLoS genetics
    Species: C. elegans
    Sample Types: Tissue Homogenates
    Applications: Bioassay
  2. The molecular network of the proteasome machinery inhibition response is orchestrated by HSP70, revealing vulnerabilities in cancer cells
    Authors: M Oro?, M Grochowski, A Jaiswar, J Legierska, K Jastrz?bsk, M Nowak-Niez, M Ko?os, W Ka?miercza, T Olesi?ski, M Lenarcik, M Cybulska, M Mikula, A ?ylicz, M Mi?czy?ska, K Zettl, JR Wi?niewski, D Walerych
    Cell Reports, 2022-09-27;40(13):111428.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  3. Inhibition of mitochondrial LonP1 protease by allosteric blockade of ATP -binding and -hydrolysis via CDDO and its derivatives
    Authors: J Lee, AK Pandey, S Venkatesh, J Thilagavat, T Honda, K Singh, CK Suzuki
    The Journal of Biological Chemistry, 2022-02-11;0(0):101719.
  4. POT1-TPP1 binding stabilizes POT1, promoting efficient telomere maintenance
    Authors: T Aramburu, J Kelich, C Rice, E Skordalake
    Computational and structural biotechnology journal, 2022-01-11;20(0):675-684.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  5. Typically inhibiting USP14 promotes autophagy in M1-like macrophages and alleviates CLP-induced sepsis
    Authors: F Xu, Y Ma, W Huang, J Gao, M Guo, J Li, L Kong, G Liang, R Du, Q Xu, X Wu
    Cell Death Dis, 2020-08-20;11(8):666.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  6. A new gold(I) complex-Au(PPh3)PT is a deubiquitinase inhibitor and inhibits tumor growth
    Authors: X Li, Q Huang, H Long, P Zhang, H Su, J Liu
    EBioMedicine, 2018-12-05;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  7. MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana
    Authors: JH Kim, SK Cho, TR Oh, MY Ryu, SW Yang, WT Kim
    Proc. Natl. Acad. Sci. U.S.A., 2017-10-30;114(46):E10009-E10017.
    Applications: Bioassay
  8. Diabetogenic agent alloxan is a proteasome inhibitor
    Authors: W Zhou, L Wei, T Xiao, C Lai, M Peng, L Xu, X Luo, S Deng, F Zhang
    Biochem. Biophys. Res. Commun., 2017-05-11;0(0):.
    Applications: Bioassay
  9. Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB(+1)
    Authors: Michal Chojnacki
    FEBS Lett, 2016-11-22;590(24):4573-4585.
    Applications: Bioassay
  10. Proteasome addiction defined in Ewing's sarcoma is effectively targeted by a novel class of 19S proteasome inhibitors
    Authors: Neerav N Shukla
    Cancer Res, 2016-06-02;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  11. Arabidopsis PROTEASOME REGULATOR1 is required for auxin-mediated suppression of proteasome activity and regulates auxin signalling
    Authors: BJ Yang, XX Han, LL Yin, MQ Xing, ZH Xu, HW Xue
    Nat Commun, 2016-04-25;7(0):11388.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  12. Proteasome inhibition and oxidative reactions disrupt cellular homeostasis during heme stress.
    Authors: Vallelian F, Deuel J, Opitz L, Schaer C, Puglia M, Lonn M, Engelsberger W, Schauer S, Karnaukhova E, Spahn D, Stocker R, Buehler P, Schaer D
    Cell Death Differ, 2014-10-10;22(4):597-611.
    Applications: Bioassay
  13. RedOx status, proteasome and APEH: insights into anticancer mechanisms of t10,c12-conjugated linoleic acid isomer on A375 melanoma cells.
    Authors: Bergamo P, Cocca E, Palumbo R, Gogliettino M, Rossi M, Palmieri G
    PLoS ONE, 2013-11-19;8(11):e80900.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  14. ERalpha phosphorylation at Y537 by Src triggers E6-AP-ERalpha binding, ERalpha ubiquitylation, promoter occupancy, and target gene expression.
    Authors: Sun J, Zhou W, Kaliappan K, Nawaz Z, Slingerland J
    Mol Endocrinol, 2012-08-03;26(9):1567-77.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay

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