A8724
ADP-ribosyltransferase C3 from Clostridium botulinum
Sinónimos:
Botulinum neurotoxin C3, C3 Exoenzyme, C3 Exotoxin, C3 Transferase
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About This Item
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Application
ADP-ribosyltransferase C3 from Clostridium botulinum may be used to study cellular signaling and G protein expression .
Biochem/physiol Actions
ADP-ribosyltransferase C3 from Clostridium botulinum ribosylates rho in eukaryotes in the presence of NAD. The ADP-ribosylating exoenzyme forms a single major 25 kDA (approx.) band with SDS electrophoresis. The enzyme labels 21-24 kDa proteins in tissues such as the human platelet membranes.
Ribosylates rho in eukaryotes in the presence of NAD.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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Plant molecular biology, 82(4-5), 339-351 (2013-04-30)
Besides the KU-dependent classical non-homologous end-joining (C-NHEJ) pathway, an alternative NHEJ pathway first identified in mammalian systems, which is often called the back-up NHEJ (B-NHEJ) pathway, was also found in plants. In mammalian systems PARP was found to be one
Journal of biochemistry, 109(3), 428-435 (1991-03-01)
A GTP-binding protein with an Mr of 24,000 was purified from a cholate extract of bovine brain membranes in addition to the previously reported alpha beta gamma-trimeric GTP-binding proteins (G proteins). Partial amino acid sequence analysis of the purified 24-kDa
European journal of biochemistry, 172(2), 445-450 (1988-03-01)
A novel ADP-ribosyltransferase C3 was purified to homogeneity from filtrates of certain strains of Clostridium botulinum type C by ammonium sulfate precipitation, gel filtration, ion-exchange chromatography and heat treatment. The molecular mass of botulinum ADP-ribosyltransferase C3 was found to be
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Tankyrases constitute potential drug targets for cancer and myelin-degrading diseases. We have applied a structure- and biophysics-driven fragment-based ligand design strategy to discover a novel family of potent inhibitors for human tankyrases. Biophysical screening based on a thermal shift assay
Cancer science, 105(4), 370-388 (2014-02-04)
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