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BirA Biotin-protein Ligase
Biotin-protein ligase (EC 6.3.4.15) activates biotin to form biotinyl 5' adenylate and transfers the biotin to biotin-accepting proteins. It also functions as a biotin operon repressor.
Description
Botulinum neurotoxin type A is one of the 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 light chains are active proteases. However, they are not toxic because they cannot enter into host cells in the absence of the heavy chains.
Full Name
Botulinum neurotoxin light chain
Source
E. coli
Species
Clostridium botulinum
Accession #
Q45894
Molecule Weight
The recombinant BXT LC consists of amino acids (1-425) and has a predicted molecular mass of 50 kDa.
Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1 EU per μg of the protein as determined by the LAL method
Activity
Measured by its ability to cleave the fluorogenic peptide substrate, SNAPtide. The specific activity is >1 pmol/min/µg, as measured under the described conditions.
Storage
-80 °C, avoid repeated freeze-thaw cycles
Storage Buffer
PBS
BTXLC-100
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Botulinum neurotoxin type A is one of the seven serotypes of Botulinum Neurotoxins (BoNTs) produced by various strains of Clostridium botulinum.