Recombinant Human Ubiquitin w/K63 only N-Term Biotin, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Ubiquitin w/K63 only N-Term Biotin, CF Summary

Details of Functionality
The lysine residue utilized for Ubiquitin chain formation is functionally important. Single lysine Ubiquitin mutants are ideal for investigating biological processes involving specific Ubiquitin chain linkages. Biotinylated Recombinant Human Ubiquitin K63-only allows for the formation of only K63-linked Ubiquitin chains. Reaction conditions will need to be optimized for each specific application. We recommend using Biotinylated Recombinant Human Ubiquitin K63-only in conjunction with native Ubiquitin at a combined concentration of 10-50 μM with a 1:2 to 1:20 ratio of mutant Ubiquitin:native Ubiquitin. The resulting poly-Ubiquitin chains can be visualized/quantitated with avidin-linked detection reagents.
Source
E. coli-derived human Ubiquitin protein
Accession #
Protein/Peptide Type
Recombinant Proteins
Gene
UBB
Purity
>95%, by PAGE

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 reconstitution.
Purity
>95%, by PAGE

Notes

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

Alternate Names for Recombinant Human Ubiquitin w/K63 only N-Term Biotin, CF

  • RPS27A
  • UBA52
  • UBB ubiquitin B
  • UBB
  • UBC
  • Ubiquitin

Background

Ubiquitin is a 76 amino acid (aa) protein that is ubiquitously expressed in all eukaryotic organisms. Ubiquitin is highly conserved with 96% aa sequence identity shared between human and yeast Ubiquitin, and 100% aa sequence identity shared between human and mouse Ubiquitin (1). In mammals, four Ubiquitin genes encode for two Ubiquitin-ribosomal fusion proteins and two poly-Ubiquitin proteins. Cleavage of the Ubiquitin precursors by deubiquitinating enzymes gives rise to identical Ubiquitin monomers each with a predicted molecular weight of 8.6 kDa. Conjugation of Ubiquitin to target proteins involves the formation of an isopeptide bond between the C-terminal glycine residue of Ubiquitin and a lysine residue in the target protein. This process of conjugation, referred to as ubiquitination or ubiquitylation, is a multi-step process that requires three enzymes: a Ubiquitin-activating (E1) enzyme, a Ubiquitin-conjugating (E2) enzyme, and a Ubiquitin ligase (E3). Ubiquitination is classically recognized as a mechanism to target proteins for degradation and as a result, Ubiquitin was originally named ATP-dependent Proteolysis Factor 1 (APF-1) (2,3). In addition to protein degradation, ubiquitination has been shown to mediate a variety of biological processes such as signal transduction, endocytosis, and post-endocytic sorting (4-7).

Produced via a proprietary process resulting in a single Biotin modification exclusively on the N-terminus of Ubiquitin. This site-specific modification results in a Ubiquitin that is fully functional at the C-terminus, and with the full compliment of reactive lysines to allow for poly-Ubiquitin chain incorporation. Detection with Avidin-linked reagents allows for a higher efficiency and detection sensitivity than with Anti-Ubiquitin antibodies. Ideal as an alternative Toradio-labeled Ubiquitin. This Ubiquitin mutant contains only a single lysine (K63) with all other lysines mutated to arginine, and is able to form poly-Ubiquitin chains with other Ubiquitin molecules via the K63 lysine only.

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Article Review: Glucose-induced transcriptional regulation in cancer
Epigenetic mechanisms have been implicated in many physiological and pathophysiological processes. Among these, histone modifications including methylation, phosphorylation, acetylation and ubiquitination, significantly modify gene expression. In c...  Read full blog post.

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The protein PINK1 is a mitochondrial-located serine/threonine kinase (PTK) that maintains organelle function and integrity. It not only protects organelles from cellular stress, but it also uses the selective auto-phagocytosis process for cleaning and...  Read full blog post.

Ubiquitin-Mediated Degradation of Cellular Proteins: The Kiss of Death
Ubiquitin is an abundant and essential cellular 9-kd protein that is conserved across evolution from yeast to humans. Ubiquitin is used by cells as a covalent modifier of other proteins both to activate their function and to target them for degradatio...  Read full blog post.

Using Ubiquitin Antibodies in Various Disease Research
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The Latest Research on IBR-type E3 Ubiquitin Ligases
E3 ubiquitin ligases are standards in most antibody catalogs. These proteins are essential to the process of ubiquitination, which is expressed in protein pathways throughout the body and is often linked to disease states. It is widely used as a bioma...  Read full blog post.

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Bioinformatics

Gene Symbol UBB
Uniprot