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662116 Ubiquitin Conjugating Enzyme Set

Ubiquitin Conjugating Enzyme Set: Malzeme Güvenlik Bilgi Formu (MSDS) veya SDS, Analiz Sertifikası (COA) ve Kalite Uygunluk Sertifikası (COQ), dosyalar, broşürler ve diğer dokümanlar.
662116
  
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      Overview

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      Contains 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
      Global Trade Item Number
      Catalogue Number GTIN
      662116 0

      Documentation

      Ubiquitin Conjugating Enzyme Set MSDS

      Title

      Safety Data Sheet (SDS) 

      Ubiquitin Conjugating Enzyme Set 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 Avoid freeze/thaw
      ≤ -70°C
      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.