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A8724

Sigma-Aldrich

ADP-ribosyltransferase C3 from Clostridium botulinum

Synonym(s):

Botulinum neurotoxin C3, C3 Exoenzyme, C3 Exotoxin, C3 Transferase

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352204
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form

powder

Quality Level

storage temp.

2-8°C

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Application

ADP-ribosyltransferase C3 from Clostridium botulinum may be used to study cellular signaling and G protein expression [1].

Biochem/physiol Actions

ADP-ribosyltransferase C3 from Clostridium botulinum ribosylates rho in eukaryotes in the presence of NAD.[1] 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.[2]
Ribosylates rho in eukaryotes in the presence of NAD.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Qi Jia et al.
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
Jonathan Ledermann et al.
The Lancet. Oncology, 15(8), 852-861 (2014-06-03)
Maintenance monotherapy with the PARP inhibitor olaparib significantly prolonged progression-free survival (PFS) versus placebo in patients with platinum-sensitive recurrent serous ovarian cancer. We aimed to explore the hypothesis that olaparib is most likely to benefit patients with a BRCA mutation.
Noriko Hosoya et al.
Cancer science, 105(4), 370-388 (2014-02-04)
Cancer chemotherapy and radiotherapy are designed to kill cancer cells mostly by inducing DNA damage. DNA damage is normally recognized and repaired by the intrinsic DNA damage response machinery. If the damaged lesions are successfully repaired, the cells will survive.
Françoise Dantzer et al.
The FEBS journal, 280(15), 3508-3518 (2013-06-05)
Poly(ADP-ribose) polymerases (PARPs) are enzymes that transfer poly(ADP-ribose) (PAR) groups to target proteins, and thereby affect various nuclear and cytoplasmic processes. The activity of PARP family members, such as PARP1 and PARP2, is tied to cellular signalling pathways, and, through
J Michels et al.
Oncogene, 33(30), 3894-3907 (2013-09-17)
Poly(ADP-ribose) polymerase (PARP) inhibitors have raised high expectations for the treatment of multiple malignancies. PARP inhibitors, which can be used as monotherapies or in combination with DNA-damaging agents, are particularly efficient against tumors with defects in DNA repair mechanisms, in

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