322326 | Diphtheria Toxin, Unnicked, Corynebacterium diphtheriae - Calbiochem

322326
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      322326-1MG
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          Glass bottle 1 mg
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          Description
          OverviewCatalyzes ADP-ribosylation of eukaryotic aminoacyltransferase II (EF2) using NAD as substrate, thereby inhibiting protein synthesis. May also induce internucleosomal breakdown. Causes DNA fragmentation and cytolysis in U937 cells. Activation requires nicking with a protease followed by reduction with DTT.
          Catalogue Number322326
          Brand Family Calbiochem®
          References
          ReferencesKochi, S.K., and Collier, R.J. 1993. Exp. Cell Res. 208, 296.
          Chang, M.P., et al. 1989. J. Biol. Chem. 264, 15261.
          Pappenheimer, A.M., Jr. 1977. Annu. Rev. Biochem. 46, 69.
          Ittelson, T.R., and Gill, D.M. 1973. Nature 242, 330.
          Uchida, T., et al. 1973. J. Biol. Chem. 248, 3851.
          Pappenheimer, A.M., et al. 1972. Immunochem. 9, 891.
          Uchida, T., et al. 1972. Science 175, 901.
          Bowman, C.G., and Bonventre, P.F. 1970. J. Exp. Med. 131, 659.
          Baseman, J.B., et al. 1970. J. Exp. Med. 132, 1138.
          Gill, D.M., et al. 1969. J. Exp. Med. 129, 1.
          Gill, D.M., et al. 1969. Cold Spring Harbor Symp. Quant. Biol. 34, 589.
          Honjo, J., et al. 1968. J. Biol. Chem. 243, 3553.
          Product Information
          ATP CompetitiveN
          FormSolid
          FormulationLyophilized from sterile 10 mM Tris, 1 mM EDTA, pH 7.5.
          ReversibleN
          Applications
          Biological Information
          Biological activityNote: Toxicity may vary by lot of toxin. Each laboratory should determine the optimum dosage for each particular application.
          Primary TargetEukaryotic aminoacyltransferase II (EF2)
          PurityMajor band (under reducing conditions) of ~63 kDa
          Physicochemical Information
          Cell permeableN
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          RTECSXW5807200
          Safety Information
          R PhraseR: 20/21/22

          Harmful by inhalation, in contact with skin and if swallowed.
          S PhraseS: 36

          Wear suitable protective clothing.
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Ambient Temperature Only
          Toxicity Harmful
          Storage +2°C to +8°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot, quickly freeze on dry ice, and freeze (-70°C). Subsequent thawing should be carried out only at room temperature. For assays employing very low concentrations of diphtheria toxin, the use of a carrier protein, such as BSA or HSA, is recommended.
          Canadian export regulations Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          322326

          References

          Reference overview
          Kochi, S.K., and Collier, R.J. 1993. Exp. Cell Res. 208, 296.
          Chang, M.P., et al. 1989. J. Biol. Chem. 264, 15261.
          Pappenheimer, A.M., Jr. 1977. Annu. Rev. Biochem. 46, 69.
          Ittelson, T.R., and Gill, D.M. 1973. Nature 242, 330.
          Uchida, T., et al. 1973. J. Biol. Chem. 248, 3851.
          Pappenheimer, A.M., et al. 1972. Immunochem. 9, 891.
          Uchida, T., et al. 1972. Science 175, 901.
          Bowman, C.G., and Bonventre, P.F. 1970. J. Exp. Med. 131, 659.
          Baseman, J.B., et al. 1970. J. Exp. Med. 132, 1138.
          Gill, D.M., et al. 1969. J. Exp. Med. 129, 1.
          Gill, D.M., et al. 1969. Cold Spring Harbor Symp. Quant. Biol. 34, 589.
          Honjo, J., et al. 1968. J. Biol. Chem. 243, 3553.
          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.

          Revision14-July-2017 JSW
          DescriptionCatalyzes ADP-ribosylation of eukaryotic aminoacyltransferase II (EF2) using NAD as substrate, thereby inhibiting protein synthesis. May also induce internucleosomal breakdown. Causes DNA fragmentation and cytolysis in U937 cells. Activation requires nicking with a protease followed by reduction with DTT. Diphtheria toxin, secreted by certain strains of Corynebacterium diphtheriae, catalyzes the ADP-ribosylation of eukaryotic aminoacyl transferase II (EF2) using NAD as a substrate. The reaction is the basis of its toxicity towards eukaryotic organisms.

          Diphtheria toxin, synthesized and excreted as a proenzyme, is composed of a single polypeptide chain of 63 kDa. For its enzymatic activity to be expressed, the toxin must undergo two covalent alterations in structure. First, a mild proteolysis results in the formation of an enzymatically inactive "nicked toxin," which consists of two major fragments (A and B) linked by a disulfide bond. Reduction of the nicked toxin with thiols (DTT) releases the enzymatically active N-terminal A fragment (24 kDa). The C-terminal B fragment (39 kDa) has no apparent enzymatic activity. The B fragment is required for toxicity and is responsible for recognizing and binding of the toxin to cell surface receptors. Diphtheria toxin is purified from Corynebacterium diphtheriae Park Williams strain 8 by a modified method of Pappenheimer, et al. As assessed by disc electrophoresis run at alkaline pH under non-denaturing conditions, this preparation migrates as a major band at 63 kDa, corresponding to the intact toxin. Two faster, more lightly stained bands (24 and 39 kDa), corresponding to A and B fragments, may be observed. Following trypsin treatment in DTT, diphtheria toxin exhibits high activity when assayed for its ability to ADP-ribosylate EF2. The ED50 for CHO cells is determined to be about 0.4 ng/ml.
          FormSolid
          FormulationLyophilized from sterile 10 mM Tris, 1 mM EDTA, pH 7.5.
          RTECSXW5807200
          PurityMajor band (under reducing conditions) of ~63 kDa
          Biological activityNote: Toxicity may vary by lot of toxin. Each laboratory should determine the optimum dosage for each particular application.
          SolubilityAqueous buffers or H₂O. Please see vial label for lot-specific reconstitution volume.
          Storage +2°C to +8°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot, quickly freeze on dry ice, and freeze (-70°C). Subsequent thawing should be carried out only at room temperature. For assays employing very low concentrations of diphtheria toxin, the use of a carrier protein, such as BSA or HSA, is recommended.
          Toxicity Harmful
          ReferencesKochi, S.K., and Collier, R.J. 1993. Exp. Cell Res. 208, 296.
          Chang, M.P., et al. 1989. J. Biol. Chem. 264, 15261.
          Pappenheimer, A.M., Jr. 1977. Annu. Rev. Biochem. 46, 69.
          Ittelson, T.R., and Gill, D.M. 1973. Nature 242, 330.
          Uchida, T., et al. 1973. J. Biol. Chem. 248, 3851.
          Pappenheimer, A.M., et al. 1972. Immunochem. 9, 891.
          Uchida, T., et al. 1972. Science 175, 901.
          Bowman, C.G., and Bonventre, P.F. 1970. J. Exp. Med. 131, 659.
          Baseman, J.B., et al. 1970. J. Exp. Med. 132, 1138.
          Gill, D.M., et al. 1969. J. Exp. Med. 129, 1.
          Gill, D.M., et al. 1969. Cold Spring Harbor Symp. Quant. Biol. 34, 589.
          Honjo, J., et al. 1968. J. Biol. Chem. 243, 3553.