Diphtheria Toxin Protein
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- Target Alle Diphtheria Toxin Produkte
- Diphtheria Toxin
- Protein-Typ
- Native
- Biologische Aktivität
- Active
- Spezies
- Corynebacterium diphtheriae
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Quelle
- Corynebacterium diphtheriae
- Applikation
- ELISA, Western Blotting (WB), Blocking Antibody (Inhibition), Functional Studies (Func), Negative Control (NC), SDS-PAGE (SDS)
- Reinheit
- > 95 % purity by SDS-PAGE (see below, SDS-PAGE without mercaptoethanol)
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- Applikationshinweise
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1) Inhibition of protein synthesis in eucaryotic cells
2) Negative selection agent for ES cells in construction of transgenic mouse
3) Putative drug for treatment of malignant tumors such as leukemia
4) Antigen for Western blotting and ELISA
5) As a marker of Diphtheria toxin in SDS-PAGE - Kommentare
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Activity test: Addition of 20 ~30 pg/mL of Diphtheria toxin in growth medium caused 50 % lethality after 43 h in Vero cells. Nicking of Diphtheria toxin by trypsin by trypsin and reduction by dithiothreitol further increase the activity
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Konzentration
- 5 mg/mL
- Buffer
- 20 mM Tris-HCl ( pH 7.2), 150 mM NaCl
- Lagerung
- -80 °C
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A novel negative selection for homologous recombinants using diphtheria toxin A fragment gene." in: Analytical biochemistry, Vol. 214, Issue 1, pp. 77-86, (1994) (PubMed).
: "Diphtheria toxin." in: Annual review of biochemistry, Vol. 46, pp. 69-94, (1977) (PubMed).
: "Diphtheria toxin and related proteins. 3. Reconstitution of hybrid "diphtheria toxin" from nontoxic mutant proteins." in: The Journal of biological chemistry, Vol. 248, Issue 11, pp. 3851-4, (1973) (PubMed).
: "
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A novel negative selection for homologous recombinants using diphtheria toxin A fragment gene." in: Analytical biochemistry, Vol. 214, Issue 1, pp. 77-86, (1994) (PubMed).
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- Target
- Diphtheria Toxin
- Abstract
- Diphtheria Toxin Produkte
- Hintergrund
- This Diphtheria toxin was highly purified from the growth media of Corynebacterium diphtheriae strain PW8 as mostly unnicked form. Diphtheria toxin is a single polypeptide chain of 535 amino acids (58 kD) and nicked by cellular protease like furin to give fragments A (N-terminal, 21 kDa) and B (C-terminal, 37 kDa) which are linked by disulfide bridges. Binding to the cell surface of frgment B allows fragment A to penetrate the host cell. Fragment A catalyzes the ADP-ribosylation of eucaryotic elongation factor-2 (eEF2) by using NAD as a substrate, thus inactivating eEF2 and inhibiting protein synthesis.
- UniProt
- Q5PY51
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