Key Details
| Catalog | MAS-0124-YJ43 |
| Applications | ELISA |
| Host | Sheep |
| Reactivity | C. botulinum |
| Clonality | Monoclonal |
| Conjugations | Conjugation could be customized |
| Sub CAT. | Applications | Clone | Conjugations | Endotoxin Level | Size | Quantity | |
|---|---|---|---|---|---|---|---|
| MAS-0124-YJ43-A | ELISA | M56 |
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Overview
Properties
Target
Overview
| Description | Clone M56 is a Sheep monoclonal IgG recognizes C. botulinum BoNT/A Heavy Chain. It has potential to be used for BoNT/A detection. |
| Reactivity | C. botulinum |
| Applications | ELISA |
| Host | Sheep |
| Immunogen | Recombinant BoNT/A1 heavy chain carboxyl end (A-HC) |
| Isotype | Sheep IgG |
| Clonality | Monoclonal |
| Clone | M56 |
| Dilutions | ELISA: 0.1-1000 ng/mL |
Properties
| Expression Host | HEK293F/CHO |
| Conjugations | Conjugation could be customized |
| Purification | Protein A/G affinity purified is the regular method |
| Purity | SDS-PAGE> 95% |
| Endotoxin Level | Endotoxin level could be customized |
| Form | Liquid (frequently-used) or lyophilized |
| Concentration | About 1mg/ml. There are differences between batches. Special concentration could be customized. |
| Sterility | 0.2 μM filtered |
| Buffer | See the Datasheet |
| Storage | See the Datasheet |
Target
| Target | C. botulinum BoNT/A Heavy Chain |
| Alternative Names | BoNT/A; Botulinum neurotoxin type A; C. botulinum BoNT/A Heavy Chain; BoNT; Botulinum neurotoxin; BotA; Heavy chain; HC; Clostridium botulinum |
| Introduction | 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. |
| Organism | Bacteria |
| Related Disease | Flaccid paralytic disease |
| Infections Route | Cutaneous; Inhalation; Gastrointestinal; Injection |
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