|Detection of C. botulinum BoNT‑G Light Chain by Western Blot. Western blot shows recombinant C. botulinum BoNT-G Light Chain. PVDF membrane was probed with 1 µg/mL of Sheep Anti-C. botulinum BoNT‑G Light Chain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7079) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for BoNT‑G Light Chain at approximately 52 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
BoNT-G LC (Botulinum neurotoxin serotype G light chain) is a 47 kDa member of the peptidase M27 family of molecules. It is the product of Clostridium botulinum, and inhibits neurotransmitter release from the neuromuscular junction. This is accomplished by BoNT-G binding to synaptotagmin and ganglioside, followed by its internalization and subsequent light chain-mediated cleavage of synaptobrevin/VAMP that blocks synaptic vesicle fusion with the presynaptic membrane. BoNT-G precursor is 1297 amino acids (aa) in length. Following internalization and precursor proteolytic cleavage, it assumes a mature form that contains a 442 aa N-terminal enzymatic light chain disulfide-linked to an 855 aa C-terminal receptor-binding heavy chain. The 97 kDa heavy chain creates a channel within the endosome that allows for redox rupture of the disulfide bond and entry of the enzymatic light chain into the cytosol where it generates noncovalent homodimers. Over aa 2-427, BoNT-G light chain shares 60% aa identity with BoNT-B light chain.
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