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662116 | Ubiquitin Conjugating Enzyme Set

662116
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      662116-1SET
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      Limited AvailabilityLimited Availability
      Stocked 
      Discontinued
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      Available
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          Glass bottle 1 set
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          Description
          OverviewContains 10 µg each of the following ubiquitin conjugating (E2) enzymes: GST-Fusion UbcH2 (Cat. No. 662111), His•Tag® UbcH3, GST-Fusion UbcH5a (Cat. No. 662091), GST-Fusion UbcH5b (Cat. No. 662092), His•Tag® UbcH6 (Cat. No. 662094), UbcH7, and His•Tag® UbcH10 (Cat. No. 662095). Useful for selecting the appropriate enzyme in novel reactions.
          Catalogue Number662116
          Brand Family Calbiochem®
          References
          ReferencesLin, Y., et al. 2002. J. Biol. Chem. 277, 21913.
          Hatakeyama, S., et al. 2001. J. Biol. Chem. 276, 33111.
          Pickart, C.M. 2001. Annu. Rev. Biochem. 70, 503.
          Zheng, N., et al. 2000. Cell 102, 533.
          Gonen, H., et al. 1999. J. Biol. Chem. 274, 14823.
          Product Information
          FormLiquid
          FormulationEach enzyme is supplied in 50 mM HEPES, 50 mM NaCl, 1 mM DTT, 10% glycerol, pH 7.8.
          Applications
          Biological Information
          Purity≥95% by SDS-PAGE
          Physicochemical Information
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Dry Ice Only
          Toxicity Standard Handling
          Storage ≤ -70°C
          Avoid freeze/thaw Avoid freeze/thaw
          Do not freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze -70°C.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          662116

          References

          Reference overview
          Lin, Y., et al. 2002. J. Biol. Chem. 277, 21913.
          Hatakeyama, S., et al. 2001. J. Biol. Chem. 276, 33111.
          Pickart, C.M. 2001. Annu. Rev. Biochem. 70, 503.
          Zheng, N., et al. 2000. Cell 102, 533.
          Gonen, H., et al. 1999. J. Biol. Chem. 274, 14823.
          Data Sheet

          Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

          Revision16-September-2008 RFH
          DescriptionProteasomes are large multi-subunit protease complexes, localized in the nucleus and cytosol, that selectively degrade intracellular proteins. They play a major role in the degradation of many proteins involved in cell cycling, proliferation, and apoptosis. A vast majority of short-lived proteins are degraded by the ubiquitin-proteasome pathway. A protein marked for degradation is covalently attached to multiple molecules of ubiquitin, a highly conserved 76-amino acid (8.6 kDa) protein, by a multi-enzymatic system consisting of Ubiquitin-activating (E1), Ubiquitin-conjugating (E2), and the Ubiquitin-ligating (E3) enzymes. The E1 activates a Ubiquitin monomer at its C-terminal cysteine residue to a high-energy thiolester bond which is then transferred to a reactive cysteine residue of the E2 enzyme. The final transfer of ubiquitin to e-amino group of a reactive lysine residue of substrate proteins is brought about by the E3 enzyme. Ubiquitinated protein is then escorted to the 26S proteasome where it undergoes final degradation and the ubiquitin is released and recycled.

          Though the E1 protein is highly conserved, several species of E2 and E3 enzymes have been characterized. The various E2 and E3 proteins function in cognate pairs and provide specificity in the ubiquitination process. The E3 proteins are thought to determine the substrate specificity of the ubiquitination and they catalyze the formation of an isopeptide bond between the substrate protein (or ubiquitin molecule) lysine residue and the C terminus of ubiquitin, using either the HECT domain or the RING finger domain. U box proteins may constitute a third family of E3 enzymes with different specificities for E2 enzymes. A recently identified conjugation factor, E4, contains the U box domain and may reflect a specialized type of E3 activity.

          The E2 proteins identified thus far are relatively small in size, ranging from 18-21 kDa. They must contain structural features that allow them to interact with the conserved elements of the system, E1 and ubiquitin, and yet also specifically interact with the cognate E3 and the target protein. Structural studies have shown that both the HECT domain and the RING domain of E3s recognize a common motif in E2 proteins. A rigid coupling between the peptide binding and E2 binding domains of the RING E3 c-Cbl, and a conserved surface channel leading from the peptide to the E2 active site, suggests that RING E3s may function as scaffolds that position the substrate and the E2 enzyme optimally for ubiquitin transfer4. E2 enzymes that have the active site cysteine mutated to serine are incapable of binding ubiquitin and interfere with the degradation pathway.






          FormLiquid
          FormulationEach enzyme is supplied in 50 mM HEPES, 50 mM NaCl, 1 mM DTT, 10% glycerol, pH 7.8.
          Purity≥95% by SDS-PAGE
          Storage ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze -70°C.
          Toxicity Standard Handling
          ReferencesLin, Y., et al. 2002. J. Biol. Chem. 277, 21913.
          Hatakeyama, S., et al. 2001. J. Biol. Chem. 276, 33111.
          Pickart, C.M. 2001. Annu. Rev. Biochem. 70, 503.
          Zheng, N., et al. 2000. Cell 102, 533.
          Gonen, H., et al. 1999. J. Biol. Chem. 274, 14823.