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Anti-Botulinum Neurotoxin Type A/BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981)

1 Citation
Secondary Structure - Anti-Botulinum Neurotoxin Type A / BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981) - Antibodies.com
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Shipping Information

$40
Dispatched from St. Louis, MO.
Lead Time: 20-35 business days.

  • Specifications

Name
Anti-Botulinum Neurotoxin Type A/BoNT A Light Chain Aptamer [S132B-C22] (Biotin)
Description
Synthetic DNA aptamer to Botulinum Neurotoxin Type A/BoNT A Light Chain [S132B-C22] (Biotin).
Specificity
Tested for specificity to His-Sec7, His-ERK2, streptavidin, and lysozyme. The aptamer had 5% retention to lysozyme and 3% retention to His-Sec7.
Aptamer ID
S132B-C22
Conjugate

Biotin

Aptamer Resuspension
Resuspend to 100µM with 10mM Tris-HCl, pH 7.5, and 0.1mM EDTA.
Apatmer Binding Conditions
Phosphate Buffered Saline, pH 7.4, 300mM Sodium Chloride, 3mM Magnesium Chloride, 5mM DTT, 1mg/ml Bovine Serum Albumin, and 0.2 % Tween, 1mg/ml Heparin. Binding Temperature: 25°C.
Sequence
dGpdGpdGpdApdGpdGpdApdGpdGpdApdGpdApdGpdApdTpdGpdTpdGpdApdApdCpdTpdTpdGpdApdCpdApdGpdCpdGpdTpdGpdCpdCpdTpdApdGpdApdApdGpdTpdCpdCpdApdApdGpdCpdTpdTpdApdApdApdTpdApdApdCpdCpdApdCpdGpdCpdTpdCpdGpdApdCpdApdApdGpdCpdApdGpdApdApdApdCpdTpdCpdTpdApdCpdApdCpdTpdGpdGpdApdCpdTpdGpdGpdCpdGp
Aptamer Length
93 nt
Aptamer Molecular Weight (Da)
28,858.79 Da
Aptamer Affinity
Affinity (Kd) = 87 nM
Extinction Coefficient
924400 M-1cm-1
Purification
HPLC
Product Form
Lyophilized
Concentration
Reconstitution dependent.
Formulation
Lyophilized from nuclease-free water (no residual salts).
Storage
Shipped at 4°C. Lyophilized: Store at -20°C. Reconstituted: Store short term at 4°C (i.e. use within days) or aliquot and store at -20°C (medium term: i.e. use within weeks) or -80°C long term. Avoid freeze/thaw cycles.
Product Notes
Anti-Botulinum Neurotoxin Type A/BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981) is a replica of the aptamer described in PMID: 20452328.
General Notes
Aptamers have not been validated by Antibodies.com and they need to be tested/evaluated under identical conditions to which they were reported in the literature including, but not limited to, temperature and matrix/buffer conditions. All aptamers are manufactured on request and have a lead time of 20-35 business days.
Disclaimer
This product is for research use only. It is not intended for diagnostic or therapeutic use.

  • Scientific Validation DataValidation Data (1)

Secondary Structure - Anti-Botulinum Neurotoxin Type A / BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981) - Antibodies.comEnlarge Image

Anti-Botulinum Neurotoxin Type A/BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981)

Secondary structure of Anti-Botulinum Neurotoxin Type A / BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981), with a dG of -7.449 kcal/mol.

  • Product Citations (1)

PubMed LogoView Publication
In vitro selection of RNA aptamers that inhibit the activity of type A botulinum neurotoxin
This publication cites Anti-Botulinum Neurotoxin Type A/BoNT A Light Chain Aptamer [S132B-C22] (Biotin) (A320981).
Article Abstract

The category A agent, botulinum neurotoxin (BoNT), is the most toxic molecule known to mankind. The endopeptidase activity of light chain domain of BoNT is the cause for the inhibition of the neurotransmitter release and the flaccid paralysis that leads to lethality in botulism. Currently, antidotes are not available to reverse the flaccid paralysis caused by BoNT. In the present study, we have identified three RNA aptamers through SELEX-process, which bind strongly to the light chain of type A BoNT (BoNT/A) and inhibit the endopeptidase activity, with IC(50) in low nM range. Inhibition kinetic studies reveal low nM K(I) and non-competitive nature of their inhibition. Aptamers are unique group of molecules as therapeutics, and this is first report of their development as an antidote against botulism. These data on K(I) and IC(50) strongly suggest that the aptamers have strong potential as antidotes that can reverse the symptom caused by BoNT/A.

View Publication
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