AQUApure Tetra-Ub Chains (K63-linked) Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

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AQUApure Tetra-Ub Chains (K63-linked) Protein, CF Summary

Details of Functionality

Ubiquitin chains vary in length, linkage, and function. K63-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.

E. coli-derived human Tetra-Ubiquitin protein
Accession #
Protein/Peptide Type
AQUApure Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


Ub-AQUA analysis:

K63:    99.04%

K11:      0.76%

K6 :       0.13%

All other linkages ≤ 0.04%


Theoretical MW
34 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.
Read Publications using
UC-310B in the following applications:

Packaging, Storage & Formulations

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.
1 mg/ml (29 μM) in sterile, deionized water
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


Ub-AQUA analysis:

K63:    99.04%

K11:      0.76%

K6 :       0.13%

All other linkages ≤ 0.04%


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

Alternate Names for AQUApure Tetra-Ub Chains (K63-linked) Protein, CF

  • HEL-S-50
  • TetraUbiquitin
  • Tetra-Ubiquitin
  • Ub4
  • UBB
  • ubiquitin B


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.

K63-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.


  1. Kirkpatrick D.S. et al. (2006) Nat Cell Biol.  8: 700-10
  2. Ordureau, A. et al. (2014) Mol. Cell  56: 360–375
  3. Ordureau, A. et al. (2015) Pro. Nat. Acad. of Sci. USA 112: 6637–6642
  4. Phu L. et al. (2011) Mol Cell Proteomics  10: M110.003756
  5. Wall C.E. et al. (2019) Cell Reports  29: 3280

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Publications for Tetra-Ubiquitin (UC-310B)(8)

We have publications tested in 3 confirmed species: Human, N/A, Plant - Oryza sativa (Rice).

We have publications tested in 2 applications: Bioassay, Standard.

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Plant - Oryza sativa (Rice)
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Showing Publications 1 - 8 of 8.
Publications using UC-310B Applications Species
N Manczyk, G Veggiani, J Teyra, AW Strilchuk, SS Sidhu, F Sicheri The ubiquitin interacting motifs of USP37 act on the proximal Ub of a di-Ub chain to enhance catalytic efficiency Sci Rep, 2019;9(1):4119. 2019 [PMID: 30858488] (Bioassay) Bioassay
Y Masuda, S Mitsuyuki, R Kanao, A Hishiki, H Hashimoto, C Masutani Regulation of HLTF-mediated PCNA polyubiquitination by RFC and PCNA monoubiquitination levels determines choice of damage tolerance pathway Nucleic Acids Res., 2018;0(0):. 2018 [PMID: 30335157] (Standard, N/A) Standard N/A
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 USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization Nat Commun, 2018;9(1):1285. 2018 [PMID: 29599486] (Bioassay) Bioassay
P Haahr, N Borgermann, X Guo, D Typas, D Achuthanku, S Hoffmann, R Shearer, TK Sixma, N Mailand ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability Mol. Cell, 2018;0(0):. 2018 [PMID: 29576528] (Bioassay, Human) Bioassay Human
Y Zhao, MC Mudge, JM Soll, RB Rodrigues, AK Byrum, EA Schwarzkop, TR Bradstreet, SP Gygi, BT Edelson, N Mosammapar OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-Dependent Signaling Mol. Cell, 2018;69(3):505-516.e5. 2018 [PMID: 29395066] (Bioassay, Human) Bioassay Human
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 Novel polyubiquitin imaging system, PolyUb-FC, reveals that K33-linked polyubiquitin is recruited by SQSTM1/p62 Autophagy, 2017;0(0):1-43. 2017 [PMID: 29164995] (Bioassay, Human) Bioassay Human
S Wang, K Wu, Q Qian, Q Liu, Q Li, Y Pan, Y Ye, X Liu, J Wang, J Zhang, S Li, Y Wu, X Fu Non-canonical regulation of SPL transcription factors by a human OTUB1-like deubiquitinase defines a new plant type rice associated with higher grain yield Cell Res., 2017;27(9):1142-1156. 2017 [PMID: 28776570] (Bioassay, Plant - Oryza sativa (Rice)) Bioassay Plant - Oryza sativa (Rice)
K Kawaguchi, K Uo, T Tanaka, M Komada Tandem UIMs confer Lys48 ubiquitin chain substrate preference to deubiquitinase USP25 Sci Rep, 2017;7(0):45037. 2017 [PMID: 28327663] (Bioassay, N/A) Bioassay N/A

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Gene Symbol UBB