AQUApure Tetra-Ub Chains (K33-linked) Protein, CF

 

Discontinued Product

UC-103 has been discontinued.
View all Tetra-Ubiquitin products.
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Citations (4)
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AQUApure Tetra-Ub Chains (K33-linked) Protein, CF Summary

Product Specifications

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

 

Ub-AQUA analysis:

K33:   95.08%

K48:     2.69%

K63:     0.90%

K11:     0.71%

All other linkages ≤ 0.38%

Activity

Ubiquitin chains vary in length, linkage, and function. K33-linked Tetra-Ubiquitin Chains (Ub4) 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
E. coli-derived human Tetra-Ubiquitin protein
Accession #
Predicted Molecular Mass
34 kDa

Product Datasheets

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UC-103

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-103

Formulation 1 mg/ml (29 μM) in sterile, deionized water.
Shipping The product is shipped with polar packs. 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 opening.
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Background: Tetra-Ubiquitin

Linkage specific Poly-Ubiquitin chains may be used as a substrate for in vitro reactions with deubiquitinating enzymes ("DUB's") that cleave the peptide or isopeptide linkage between adjacent Ubiquitin molecules. Poly-Ubiquitin chains can also be used to investigate mechanisms of binding and recognition between the chains and other proteins that contain Ubiquitin-Associated domains (UBAs), Ubiquitin-interacting motifs (UIMs), ZnF's and/or other Ubiquitin-sensing elements.

K33-linked Tetra-Ubiquitin chains are manufactured using recombinant Ubiquitin and purely enzymatic techniques to avoid the potential for contaminating synthetic intermediates. The correctness of linkage and purity of each production lot is assessed using the Absolute Quantitation of Ubiquitin method (Ub-AQUA), an LCMS-based technique that provides extremely accurate information on the composition of Poly-Ubiquitin samples.

References
  1. Kirkpatrick D.S., et al. (2006) Nat Cell Biol. 8(7): 700-10
  2. Michel, M.A. et al. (2015) Mol Cell. 58(1): 95-109
  3. Ordureau, A., et al. (2014) Mol. Cell  56(3): 360–375
  4. Ordureau, A., et al. (2015) Pro. Nat. Acad. of Sci. USA 112(21): 6637–6642
  5. Phu L., et al. (2011) Mol Cell Proteomics 10(5): M110.003756
Entrez Gene IDs
7314 (Human)
Alternate Names
HEL-S-50; TetraUbiquitin; Tetra-Ubiquitin; Ub4; UBB; ubiquitin B

Citations for AQUApure Tetra-Ub Chains (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.

4 Citations: Showing 1 - 4
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  1. Extracellular matrix stiffness determines DNA repair efficiency and cellular sensitivity to genotoxic agents
    Authors: M Deng, J Lin, S Nowsheen, T Liu, Y Zhao, PW Villalta, D Sicard, DJ Tschumperl, S Lee, J Kim, Z Lou
    Science Advances, 2020-09-11;6(37):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
    Authors: S Yang, L Liu, C Cao, N Song, Y Wang, S Ma, Q Zhang, N Yu, X Ding, F Yang, S Tian, K Zhang, T Sun, J Yang, Z Yao, S Wu, L Shi
    Nat Commun, 2018-03-29;9(1):1285.
    Applications: Bioassay
  3. 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
  4. Novel polyubiquitin imaging system, PolyUb-FC, reveals that K33-linked polyubiquitin is recruited by SQSTM1/p62
    Authors: Y Nibe, S Oshima, M Kobayashi, C Maeyashiki, Y Matsuzawa, K Otsubo, H Matsuda, E Aonuma, Y Nemoto, T Nagaishi, R Okamoto, K Tsuchiya, T Nakamura, S Nakada, M Watanabe
    Autophagy, 2018-01-24;0(0):1-43.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay

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