| Applications | WB, IP |
| Clone | 503013 |
| Clonality | Monoclonal |
| Host | Mouse |
| Conjugate | Alexa Fluor 750 |
| Immunogen | E. coli-derived recombinant Clostridium BoNT-A Light Chain Met1-Phe425 Accession # Q45894 |
| Specificity | Detects C. botulinum BoNT‑A Light Chain in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with BoNT-B light chain, BoNT-E light chain, BoNT-A heavy chain, BoNT-C1 heavy chain, or BoNT-D heavy chain is observed. |
| Isotype | IgG2a |
| Clonality | Monoclonal |
| Host | Mouse |
| Purity Statement | Protein A or G purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
Botulinum neurotoxin type A 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. However, they are not toxic because they cannot enter into host cells in the absence of the heavy chains.
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