Botulinum Neurotoxin, Type F, Light Chain, Recombinant, aa1-428
Catalog No : USB-215926
616.11€
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| Product name | Botulinum Neurotoxin, Type F, Light Chain, Recombinant, aa1-428 | ||
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| Catalog No | USB-215926 | ||
| Supplier’s Catalog No | 215926 | ||
| Supplier | US Biologicals | ||
| Source antigen | Recombinant, E. coli | ||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | 50 | ||
| Storage | -20°C | ||
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| Other names | |||
| Grade | Highly Purified | ||
| Purity | Highly Purified (~90%) | ||
| Form | Supplied as a lyophilized powder in 20mM HEPES, pH 7.4, 1.25% lactose. Reconstitute with 60ul sterile ddH2O, 0.05% TWEEN-20 or 1mg/ml BSA. | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | Highly Purified (~90%) | ||
| Description | Clostridium botulinum neurotoxins (BoNT) are among the most toxic substances known to man. Seven immunologically distinct serotypes of neurotoxin, designated types A through G (BoNT/A, BoNT/B, BoNT/C, BoNT/D, BoNT/E, BoNT/F, BoNT/G), have been identified. These neurotoxins are naturally produced complexed with one or more nontoxic neurotoxin-associated proteins (NAPs). NAPs are important to toxicity by ingestion in that they protect the neurotoxin from proteases, acidity, heat and they may also play a role in translocation across the mucosal layer. Synthesized as single 150kD polypeptide chains, the actual neurotoxin portion of the complex is subsequently activated by cleavage to produce two chains, a heavy chain and a light chain, which are linked by a single disulfide bond. For each toxin, the 50kD light chain is a zinc- dependent protease, which cleaves a single target protein essential for synaptic vesicle membrane fusion during neurotransmission. Neurotoxin types A, C, and E specifically bind to and selectively cleave the synaptosome-associated protein, SNAP-25 while types B, D, F and G cleave synaptobrevin-2, also known as VAMP-2. Cleavage of the target protein inhibits neurotransmitter release among neurons, which leads to muscular paralysis. Each toxin is easily divided into three domains that reflect the three functions important for toxicity; binding, translocation and cleavage of a specific substrate. The heavy chain is responsible for recognizing both a specific ganglioside and a specific protein receptor on the presynaptic membrane. The translocation domain portion of the heavy chain mediates the passage of light chain across the endosomal membrane and finally the target protein is cleaved by the enzymatic domain. Botulinum neurotoxins are valuable research tools in studies aimed at elucidating the mechanisms involved in vesicle trafficking and the extreme toxicity, as well as in gaining an understanding of the underlying events of synaptic transmission. In addition to studies with the 150kD holotoxin, recombinant nontoxic heavy chains can be used to evaluate the binding properties of the toxins and the recombinant nontoxic light chains can be used to screen for inhibition of the enzymatic activity of the protease domain. Source: Recombinant protein corresponding to aa1-428 from full-length Botulinum Neurotoxin type F light chain, containing ten residual aa from the affinity tag at the N-terminus, expressed in E. coli. Molecular Weight: ~50kD Biological Activity: Tested for activity in an endopeptidase assay. 20nM light chain F was able to cleave 5uM His 6-Synaptobrevin at 37°C in 20mM Tris-HCI, pH 8.0, 50mM sodium chloride. Full cleavage was achieved within 15 minutes of initiation of the reaction. Storage and Stability: Lyophilized powder may be stored at -20°C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. | ||
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