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539164 Proteasome Inhibitor Set I - Calbiochem

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539164
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概要

Replacement Information

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539164-1SETCN
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      Description
      OverviewContains 1 mg of Proteasome Inhibitor I (Cat. No. 539160), 200 µg of Lactacystin (Cat. No. 426100), and 1 mg of MG-132 (Cat. No. 474790). Supplied with a data sheet.
      Catalogue Number539164
      Brand Family Calbiochem®
      References
      ReferencesGrimm, L.M., et al. 1996. EMBO J. 15, 3835.
      Griscavage, J.M., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 3308.
      Lee, D.H., and Goldberg, A.L. 1996. J. Biol. Chem. 271, 27280.
      Oda, K., et al. 1996. Biochem. Biophys. Res. Commun. 219, 800.
      Fenteany, G., et al. 1995. Science 268, 726.
      Traenckner, E.B., et al. 1994. EMBO J. 13, 5433.
      Product Information
      FormSolid
      Quality LevelMQ100
      Applications
      ApplicationProteasome Inhibitor Set I contains 1 mg of Proteasome Inhibitor I (Cat. No. 539160), 200 µg of Lactacystin (Cat. No. 426100), and 1 mg of MG-132 (Cat. No. 474790). Supplied with a data sheet.
      Biological Information
      Primary TargetMPC
      Secondary targetNF-κB activity
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      カタログ番号 GTIN
      539164-1SETCN 04055977269482

      Documentation

      Proteasome Inhibitor Set I - Calbiochem (M)SDS

      タイトル

      英語版製品安全データシート((M)SDS) 

      Proteasome Inhibitor Set I - Calbiochem 試験成績書(CoA)

      タイトルロット番号
      539164

      参考資料

      参考資料の概要
      Grimm, L.M., et al. 1996. EMBO J. 15, 3835.
      Griscavage, J.M., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 3308.
      Lee, D.H., and Goldberg, A.L. 1996. J. Biol. Chem. 271, 27280.
      Oda, K., et al. 1996. Biochem. Biophys. Res. Commun. 219, 800.
      Fenteany, G., et al. 1995. Science 268, 726.
      Traenckner, E.B., et al. 1994. EMBO J. 13, 5433.

      カタログ

      タイトル
      Caspases and other Apoptosis Related Tools Brochure
      Proteasomes Technical Bulletin
      データシート

      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.

      Revision04-September-2008 RFH
      DescriptionProteasomes are large multi-subunit protease complexes, localized in the nucleus and cytosol, which 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 (Ubq), a highly conserved 76-amino acid (8.6 kDa) protein, which escorts it for rapid hydrolysis to the multi-component enzymatic complex known as the 26S proteasome. The proteolytic core of this complex, the 20S proteasome, contains multiple peptidase activities and functions as the catalytic machine.

      The ubiquitin-proteasome pathway plays a major role in the breakdown of abnormal proteins that result from oxidative stress and mutations that might otherwise disrupt normal cellular homeostasis. The reactive oxygen species can promote partial unfolding of the proteins, exposing its hydrophobic domains to proteolytic enzymes of the 20S complex. Rapid degradation of defective enzymes, as seen in diseases caused by metabolic abnormalities, also occurs in the proteasome. The Ubq-proteasome pathway has also been implicated in several forms of malignancy, in the pathogenesis of several genetic diseases, and in the pathology of muscle wasting. It is also involved in the destruction of proteins that participate in cell cycle progression, transcription control, signal transduction, and metabolic regulation.
      FormSolid
      Storage -20°C
      Do Not Freeze Ok to freeze
      Toxicity Standard Handling
      ReferencesGrimm, L.M., et al. 1996. EMBO J. 15, 3835.
      Griscavage, J.M., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 3308.
      Lee, D.H., and Goldberg, A.L. 1996. J. Biol. Chem. 271, 27280.
      Oda, K., et al. 1996. Biochem. Biophys. Res. Commun. 219, 800.
      Fenteany, G., et al. 1995. Science 268, 726.
      Traenckner, E.B., et al. 1994. EMBO J. 13, 5433.