AQUApure Tetra-Ub Chains (K48-linked) Protein, CF

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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AQUApure Tetra-Ub Chains (K48-linked) Protein, CF Summary

Details of Functionality

Ubiquitin chains vary in length, linkage, and function. K48-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 #
Protein/Peptide Type
AQUApure Recombinant Proteins
Gene
UBB
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

 

Ub-AQUA analysis:

K48:    99.31%

K11:      0.36%

K63:      0.19%

K6 :       0.09%

All other linkages ≤ 0.03%

Applications/Dilutions

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.
Publications
Read Publications using
UC-210B in the following applications:

Packaging, Storage & Formulations

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

 

Ub-AQUA analysis:

K48:    99.31%

K11:      0.36%

K63:      0.19%

K6 :       0.09%

All other linkages ≤ 0.03%

Notes

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

Alternate Names for AQUApure Tetra-Ub Chains (K48-linked) Protein, CF

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

Background

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.

K48-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(7): 700-10
  2. Ordureau, A., et al. (2014) Mol. Cell  56(3): 360–375
  3. Ordureau, A., et al. (2015) Pro. Nat. Acad. of Sci. USA  112(21): 6637–6642
  4. Phu L., et al. (2011) Mol Cell Proteomics  10(5): M110.003756

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UC-210B
Species: Hu
Applications: Bioactivity

Publications for Tetra-Ubiquitin (UC-210B)(9)

We have publications tested in 2 confirmed species: N/A, Oryza sativa.

We have publications tested in 2 applications: Binding Assay, Bioassay.


Filter By Application
Binding Assay
(1)
Bioassay
(7)
All Applications
Filter By Species
N/A
(5)
Oryza sativa
(1)
All Species
Showing Publications 1 - 9 of 9.
Publications using UC-210B Applications Species
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
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, Oryza sativa) Bioassay Oryza sativa
X Lu, U Nowicka, V Sridharan, F Liu, L Randles, D Hymel, M Dyba, SG Tarasov, NI Tarasova, XZ Zhao, J Hamazaki, S Murata, TR Burke, KJ Walters Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets Nat Commun, 2017;8(0):15540. 2017 [PMID: 28598414] (Bioassay, N/A) Bioassay N/A
H Tsuchiya, F Ohtake, N Arai, A Kaiho, S Yasuda, K Tanaka, Y Saeki In�Vivo Ubiquitin Linkage-type Analysis Reveals that the Cdc48-Rad23/Dsk2 Axis Contributes to K48-Linked Chain Specificity of the Proteasome Mol. Cell, 2017;66(4):488-502.e7. 2017 [PMID: 28525741] (Bioassay) Bioassay
L Lauinger, J Li, A Shostak, IA Cemel, N Ha, Y Zhang, PE Merkl, S Obermeyer, N Stankovic-, T Schafmeier, WJ Wever, AA Bowers, KP Carter, AE Palmer, H Tschochner, F Melchior, RJ Deshaies, M Brunner, A Diernfelln Thiolutin is a zinc chelator that inhibits the Rpn11 and other JAMM metalloproteases Nat. Chem. Biol., 2017;0(0):. 2017 [PMID: 28459440]
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
Huang G, Towe C, Choi L, Yonekawa Y, Bommelje C, Bains S, Rechler W, Hao B, Ramanathan Y, Singh B The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity. J Biol Chem, 2015;290(1):296-309. 2015 [PMID: 25411243] (Binding Assay, N/A) Binding Assay N/A
Zhao, Yu, Zhu, Huaiping, Zou, Ming-Hui Non-covalent interaction between polyubiquitin and GTP cyclohydrolase 1 dictates its degradation. PLoS ONE, 2012;7(9):e43306. 2012 [PMID: 22984419] (Bioassay, N/A) Bioassay N/A
Shin D, Lee S, Han S, Ren S, Kim S, Aikawa Y, Lee S Differential polyubiquitin recognition by tandem ubiquitin binding domains of Rabex-5. Biochem Biophys Res Commun, 2012;423(4):757-62. 2012 [PMID: 22705550] (Bioassay, N/A) Bioassay N/A

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Bioinformatics

Gene Symbol UBB
Entrez
Uniprot