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Di-Ubiquitin/Ub2 (K33-linked) Protein, CF

Catalog #: UC-101
11 Citations Datasheet / COA / SDS
Newer Version Available: UC-101B
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Discontinued Product

UC-101 has been discontinued and is replaced by UC-101B.

Product Details
Citations (11)
FAQs
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Summary Product Datasheets Carrier Free Reconstitution Calculator Background Related Research Areas

Di-Ubiquitin/Ub2 (K33-linked) Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Activity
Ubiquitin chains vary in length, linkage, and function. K33-linked Di-Ubiquitin Chains (Ub2) are ideal for investigating Ubiquitin-binding proteins and as substrates for Ubiquitin-specific isopeptidases. Reaction conditions will need to be optimized for each specific application. IMPORTANT: Heating this product in SDS-PAGE buffer or terminating reactions containing this product with heated SDS-PAGE buffer could lead to unexpected, high apparent molecular weight banding or smearing on gels that is not representative of product purity. For optimal results, we recommend incubation in SDS-PAGE buffer + DTT at <40 °C for 20 minutes prior to gel electrophoresis.
Source
Chemically Synthesized Di-Ubiquitin protein
Accession #
P0CG47
Predicted Molecular Mass
17 kDa

Product Datasheets

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UC-101

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.

UC-101

Formulation Lyophilized from a solution in deionized water.
Reconstitution

Reconstitute at 2 mg/mL in an aqueous solution.
Shipping The product is shipped at ambient temperature. 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, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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: Di-Ubiquitin

With a predicted molecular weight of 17 kDa, Di-Ubiquitin is composed of two Ubiquitin monomers that are covalently linked through an isopeptide bond, which typically form between a lysine residue of one Ubiquitin molecule and the C-terminal glycine residue of another Ubiquitin molecule (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively (2). Ubiquitin has seven lysine residues that can participate in the formation of poly-Ubiquitin chains. The specific lysine residue used in Ubiquitin conjugation is thought to determine the function of poly-ubiquitination in cellular processes such as protein degradation, signaling, and trafficking (3-8).

Linkage specific di-Ubiquitin is a substrate for enzymes that cleave the isopeptide linkage between two Ubiquitin molecules. It can also be used to investigate mechanism of binding and recognition by Ubiquitin-activating (E1) or Ubiquitin-conjugating (E2) enzymes, deubiquitinating enzymes, Ubiquitin ligases (E3), or other proteins that contain Ubiquitin-associated domains (UBAs) or Ubiquitin-interacting motifs (UIMs).

References
  1. Scheffner, M. et al. (1995) Nature 373:81.
  2. Sharp, P.M. & W.-H. Li (1987) Trends Ecol. Evol. 2:328.
  3. Behrends, C. & J.W. Harper (2011) Nat. Struct. Mol. Biol. 18:520.
  4. Greene, W. et al. (2012) PLoS Pathog. 8:e1002703.
  5. Henry, A.G. et al. (2012) Dev. Cell 23:519.
  6. Tong, X. et al. (2012) J. Biol. Chem. 287:25280.
  7. Wei, W. et al. (2004) Nature 428:194.
  8. Zhang, J. et al. (2012) J. Biol. Chem. 287:28646.
  9. Buchberger A., et al. (2002) Trends. Cell. Biol. 12:216-221.
  10. Cook W.J., et al. (1992) J. Biol. Chem. 267:16467-16471.
  11. El Oualid, F., et al. (2010) Angewandte Chemie. 49: 10149-10153.
  12. Fischer R.D., et al. (2003) J. Biol. Chem. 278:28976-28984.
  13. Tenno T., et al. (2004) Genes to Cells. 9:865-875.
  14. Varadan R., et al. (2002) J. Mol. Biol. 324:637-647.
  15. Varadan R., et al. (2004) J. Biol. Chem. 279:7055-7063.  
Entrez Gene IDs
7314 (Human)
Alternate Names
DiUbiquitin; Di-Ubiquitin; HEL-S-50; Ub2; UBB; ubiquitin B

Citations for Di-Ubiquitin/Ub2 (K33-linked) 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.

11 Citations: Showing 1 - 10
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  1. The ubiquitin interacting motifs of USP37 act on the proximal Ub of a di-Ub chain to enhance catalytic efficiency
    Authors: N Manczyk, G Veggiani, J Teyra, AW Strilchuk, SS Sidhu, F Sicheri
    Sci Rep, 2019-03-11;9(1):4119.
    Applications: Bioassay
  2. ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability
    Authors: P Haahr, N Borgermann, X Guo, D Typas, D Achuthanku, S Hoffmann, R Shearer, TK Sixma, N Mailand
    Mol. Cell, 2018-03-22;0(0):.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  3. OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-Dependent Signaling
    Authors: Y Zhao, MC Mudge, JM Soll, RB Rodrigues, AK Byrum, EA Schwarzkop, TR Bradstreet, SP Gygi, BT Edelson, N Mosammapar
    Mol. Cell, 2018-02-01;69(3):505-516.e5.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  4. Characterization of the deubiquitination activity and substrate specificity of the chicken ubiquitin-specific protease 1/USP associated factor 1 complex
    Authors: H Zheng, M Wang, C Zhao, S Wu, P Yu, Y Lü, T Wang, Y Ai
    PLoS ONE, 2017-11-01;12(11):e0186535.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  5. Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation
    Authors: YJ Wang, Y Bian, J Luo, M Lu, Y Xiong, SY Guo, HY Yin, X Lin, Q Li, CCY Chang, TY Chang, BL Li, BL Song
    Nat. Cell Biol., 2017-06-12;19(7):808-819.
    Applications: Control
  6. In�Vivo Ubiquitin Linkage-type Analysis Reveals that the Cdc48-Rad23/Dsk2 Axis Contributes to K48-Linked Chain Specificity of the Proteasome
    Authors: H Tsuchiya, F Ohtake, N Arai, A Kaiho, S Yasuda, K Tanaka, Y Saeki
    Mol. Cell, 2017-05-18;66(4):488-502.e7.
    Applications: Bioassay
  7. Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains
    Authors: F He, HP Wollscheid, U Nowicka, M Biancospin, E Valentini, A Ehlinger, F Acconcia, E Magistrati, S Polo, KJ Walters
    Cell Rep, 2016-03-10;14(11):2683-94.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  8. Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest).
    Authors: Hospenthal, Manuela, Mevissen, Tycho E, Komander, David
    Nat Protoc, 2015-01-29;10(2):349-61.
    Species: Human
    Sample Types: Protein
  9. USP45 deubiquitylase controls ERCC1-XPF endonuclease-mediated DNA damage responses.
    Authors: Perez-Oliva A, Lachaud C, Szyniarowski P, Munoz I, Macartney T, Hickson I, Rouse J, Alessi D
    EMBO J, 2014-12-23;34(3):326-43.
  10. The vOTU domain of highly-pathogenic porcine reproductive and respiratory syndrome virus displays a differential substrate preference.
    Authors: Deaton M, Spear A, Faaberg K, Pegan S
    Virology, 2014-03-15;454(0):247-53.
  11. Specific recognition of linear polyubiquitin by A20 zinc finger 7 is involved in NF-kappaB regulation.
    EMBO J., 2012-08-28;31(19):3856-70.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Binding Assay

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