Rec. Human Poly-Ub WT Chains (2-7) (K63-linked) Biotin, CF

Discontinued Product

UCB-330 has been discontinued.
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Rec. Human Poly-Ub WT Chains (2-7) (K63-linked) Biotin, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Activity
Ubiquitin chains vary in length, linkage, and function. K63-linked Biotinylated Poly-Ubiquitin Chains (Ub2-7) are ideal for use in assays that utilize avidin-linked reagents for visualization or quantitation. 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 Poly-Ubiquitin protein
Accession #
Predicted Molecular Mass

17 kDa (Ub2), 26 kDa (Ub3), 34 kDa (Ub4), 43 kDa (Ub5), 52 kDa (Ub6), and 60 kDa (Ub7)

Product Datasheets

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UCB-330

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.

UCB-330

Formulation X mg/ml in 50 mM HEPES pH 8.0
Reconstitution
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: Poly-Ubiquitin

Poly-Ubiquitin chains are composed of Ubiquitin monomers that are covalently linked through  isopeptide bonds, 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). Seven of the 76 aa in Ubiquitin are lysine residues that can participate in poly-Ubiquitin chain formation. Linkage through specific lysine residues is thought to serve as a signal that affects protein degradation, signaling, trafficking, and other cellular processes (3-8).

This mixture of poly-Ubiquitin chains contains di-Ubiquitin and higher MW species; mono-Ubiquitin has been removed. These chains have been modified with biotin via primary amine coupling.  This results in multiple biotinylated species modified at the N-terminus, as well as lysine residues.  Biotinylated Ubiquitin can be detected using avidin-linked reagents.

 

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.
Alternate Names
CEP80; HEL112; PolyUbiquitin; Poly-Ubiquitin; ribosomal protein S27a; RPS27A; S27A; UBA80; UBC; UBCEP1; UBCEP80

Citation for Rec. Human Poly-Ub WT Chains (2-7) (K63-linked) Biotin, 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.

1 Citation: Showing 1 - 1

  1. Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1
    Authors: Y Guo, Q Liu, E Mallette, C Caba, F Hou, J Fux, G LaPlante, A Dong, Q Zhang, H Zheng, Y Tong, W Zhang
    The Journal of Biological Chemistry, 2021-08-21;0(0):101107.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay

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