C. botulinum BoNT-D Heavy Chain Alexa Fluor® 647-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: BoNT-D Heavy Chain

BoNT-D (Botulinum neurotoxin serotype D) is produced by Clostridium botulinum and inhibits acetylcholine release from neuromuscular junctions. Notably, BoNT-D is not toxic to human cells. The 1276 amino acid (aa) BoNT-D precursor is cleaved to generate a disulfide-linked dimer of the 50‑55 kDa light chain peptidase and the 100 kDa heavy chain. The heavy chain contains receptor binding and pore forming domains. The light chain translocates through this pore to the target cell cytosol where it cleaves synaptobrevin, thus blocking synaptic vesicle fusion with the presynaptic membrane. Within aa 862-1276 of the heavy chain, BoNT-D shares 31%, 33%, and 41% aa sequence identity with BoNT-A, -B, and -C1 heavy chains, respectively.

Product Datasheets

Related Research Areas

• Metalloproteases and Regulators
• Synaptic SNAREs