Millipore Sigma Vibrant Logo
Attenzione: Ci siamo trasferiti. Non è più possibile acquistare i prodotti Merck Millipore nel sito MerckMillipore.comPer saperne di più

322326 Diphtheria Toxin, Unnicked, Corynebacterium diphtheriae - Calbiochem

Diphtheria toxin catalyzes ADP-ribosylation of eukaryotic aminoacyltransferase II (EF2) using NAD as substrate. Activation requires nicking with a protease followed by reduction with DTT.

Diphtheria Toxin, Unnicked, Corynebacterium diphtheriae - Calbiochem: MSDS (material safety data sheet) o SDS, certificato d’analisi (CoA) e certificato di qualità (CoQ), dossier, brochure e altri documenti disponibili.
322326
Purchase on Sigma-Aldrich

Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
322326-1MG Bottiglia di vetro 1 mg
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
Quality LevelMQ100
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.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Numero di catalogo GTIN
322326-1MG 07790788060923

Documentation

Diphtheria Toxin, Unnicked, Corynebacterium diphtheriae - Calbiochem MSDS

Titolo

Scheda di sicurezza (MSDS) 

Diphtheria Toxin, Unnicked, Corynebacterium diphtheriae - Calbiochem Certificati d'Analisi

TitoloNumero di lotto
322326

Riferimenti bibliografici

Panoramica delle referenze
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.
Scheda tecnica

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.