金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived, Pro2-Gly430, with an N-terminal Met and 6-His tag Accession #:P04958 N-terminal Sequence Analysis:Met Purity:>85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 µg per lane. Endotoxin Level: Predicted Molecular Mass:50 kDa SDS-PAGE:43-50 kDa, reducing conditions Activity:Measured by the cleavage of the substrate GFPuv/SNAP/VAMP in a gel-shift assay.>50% of 1 µg substrate is cleaved by 40 ng, as measured under the described conditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris, NaCl and Tween® 20.See Certificate of Analysis for details. Molecule Information: TeNT Light Chain Long Name: Tetanus Neurotoxin Type Light Chain Aliases: TeNT-LC; Tentoxylysin; tetX Entrez Gene IDs: 1061100 (C. tetani) Background: Botulinum & Tetanus Neurotoxins (BoNT and TeNT)

There are seven serotypes of Botulinum Neurotoxins (BoNTs) produced by various strains of Clostridium botulinum. BoNTs are synthesized as inactive single chain protein precursors and activated by proteolytic cleavage to generate disulfide-linked two-chain proteins. The 50 kDa light chain contains the catalytic domain, whereas the 100 kDa heavy chain contains an internal translocation domain and a receptor binding domain. BoNTs are the most potent protein toxins for humans. As zinc proteases, they cleave SNARE proteins to elicit flaccid paralysis in botulism by blocking acetylcholine release at the neuromuscular junction.

E. coli-expressed recombinant BoNT light chains are active proteases. However, they are not toxic because they cannot enter into host cells in the absence of the heavy chains.