Detects C. botulinum BoNT-E Heavy Chain in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant Heavy Chains from BoNT-A or BoNT-G is observed.

Clonality

Monoclonal

Host

Mouse

Isotype

IgG_2B

Scientific Data Images for C. botulinum BoNT-E Heavy Chain Antibody

Detection ofC. botulinumBoNT‑E Heavy Chain by Western Blot.

Western blot shows lysates of recombinantC. botulinumBoNT-E Heavy Chain Receptor Binding Domain (25 ng/lane). PVDF membrane was probed with 1 µg/mL of Mouse Anti-C. botulinumBoNT-E Heavy Chain Monoclonal Antibody (Catalog # MAB7135) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for BoNT-E Heavy Chain at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

Applications for C. botulinum BoNT-E Heavy Chain Antibody

Application

Recommended Usage

Western Blot

1 µg/mL
Sample: Recombinant C. botulinum BoNT-E Heavy Chain Receptor Binding Domain

Formulation, Preparation, and Storage

Purification

Protein A or G purified from hybridoma culture supernatant

Reconstitution

Sterile PBS to a final concentration of 0.5 mg/mL. For liquid material, refer to CoA for concentration.

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: BoNT-E Heavy Chain

Botulinum Neurotoxin Type E 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. In the absence of the heavy chains, however, they lack toxicity because they cannot enter into host cells.

References

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

Long Name

Botulinum Neurotoxin Type E Heavy Chain

Alternate Names

BoNTE Heavy Chain, Bontoxilysin-E

UniProt

P30995 (C. botulinum)

Additional BoNT-E Heavy Chain Products

Product Documents for C. botulinum BoNT-E Heavy Chain Antibody

Product Datasheets

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COA

SDS

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Product Specific Notices for C. botulinum BoNT-E Heavy Chain Antibody

For research use only

Citations
Reviews

C. botulinum BoNT-E Heavy Chain Antibody

R&D Systems, part of Bio-Techne | Catalog # MAB7135

Key Product Details

Species Reactivity

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Label

Antibody Source

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Product Specifications

Immunogen

Specificity