Reactivity | Ba-CbSpecies Glossary |
Applications | Enzyme Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to cleave the fluorogenic peptide substrate, VAMPtide. The specific activity is >20 pmol/min/μg, as measured under the described conditions. |
Source | E. coli-derived c. botulinum BoNT-B Light Chain protein Pro2-His428, with an N-terminal Met and 6-His tag |
Accession # | |
N-terminal Sequence | Met |
Protein/Peptide Type | Recombinant Enzymes |
Gene | boNT/B |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 50 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE | 47 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a 0.2 μm filtered solution in Tris, NaCl, Tween® 20 and Glycerol. |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Assay Procedure |
*Adjusted for Substrate Blank
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Botulinum Neurotoxin Type B is one of the seven serotypes of Botulinum Neurotoxins (BoNTs) produced by various strains of Clostridium botulinum (1, 2). 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 (3). 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 (2-4). E. coli expressed recombinant light chains are active proteases. In the absence of the heavy chains, however, they lack toxicity because they cannot enter into host cells.
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