Recombinant Botulinum Neurotoxin Type F Light Chain, CF

R&D Systems, part of Bio-Techne | Catalog # 7380-ZN

R&D Systems, part of Bio-Techne
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Key Product Details

  • R&D Systems E. coli-derived Recombinant Botulinum Neurotoxin Type F Light Chain (7380-ZN)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession #

P30996

Conjugate

Unconjugated

Applications

Enzyme Activity

View all BoNT-F Light Chain Proteins and Enzymes »

Product Specifications

Source

E. coli-derived c. botulinum BoNT-F Light Chain protein
Pro2-Gly420, with an N-terminal Met and 6-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

49 kDa

SDS-PAGE

48-52 kDa, reducing conditions

Activity

Measured by the cleavage of the substrate GFPuv/SNAP/VAMP in a gel-shift assay.
>40% of 1 μg substrate is cleaved by 50 ng, as measured under the described conditions.  

Formulation, Preparation and Storage

7380-ZN
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Tween® 20 and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: BoNT-F Light Chain

Botulinum Neurotoxin Type F 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 that are activated by proteolytic cleavage to create the light and heavy chains that are linked by a disulfide bond. The 50 kDa light chain contains the metalloprotease domain whereas the 100 kDa heavy chain contains a receptor binding domain and a domain required for translocation across the cell membrane (3).  BoNTs are the most toxic protein toxins known for humans.  As zinc proteases, they cleave SNARE proteins to elicit flaccid paralysis in botulism poisoning. Cleavage of the SNARE proteins results in the blocking of acetylcholine release at the neuromuscular junction (2‑4). E. coli expressed recombinant light chains are active proteases. In the absence of heavy chains, however, they lack toxicity because they cannot enter into host cells.

References

  1. Campbell, K.D. et al. (1993) J. Clin. Microbiol. 31:2255.
  2. Montecucco, C. and S. Giampietro (1993) Trends Biochem. Sci. 18:324.
  3. Turton, K. et al. (2002) Trends Biochem. Sci. 27:552.
  4. Schiavo, G. et al. (2000) Physiol. Rev. 80:717.

Long Name

Botulinum Neurotoxin Type F Light Chain

Alternate Names

BoNTF Light Chain

UniProt

P30996 (C. botulinum)

Additional BoNT-F Light Chain Products

Product Documents for Recombinant Botulinum Neurotoxin Type F Light Chain, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Botulinum Neurotoxin Type F Light Chain, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd. Tween is a registered trademark of ICI Americas.

For research use only

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