| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Tentoxylysin |
| Cas No. | |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes). The lyophilizate may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. Soluble in any conventional buffer containing 0.01 KH2PO4, 0.1% gelatin and/or 0.1% bovine serum albumin (BSA). The use of gelatin or 0.01% BSA coated/treated glassware is recommended. Centrifuge all product preparations before use (10000 x g 5 min). |
| Source | Natural protein |
| Species | |
| Storage | |
| Target |
Overview
Tetanus Toxin is a research-grade protein/peptide reagent used in research settings. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology.
Key elements and design rationale
- Molecular identity: CAS: 676570-37-9, MW: 150 kDa.
- Source / origin: Clostridium tetani.
- Quality attributes: Purity: ≥97% (HPLC); Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between Cys439-Cys467 and Cys1077-Cys1093
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
Tetanus toxin is a 150 kD protein produced by the gram positive bacteria Clostridium tetani under anaerobic condition1. Tetanus toxin is a hetrodimer of A-chain (50 kD) and B-chain (100 kD) linked by one disulfide bond2,3. The A-chain has a zinc endopeptidase activity while the B-chain has a role in toxin anchoring to neuronal membranes4.Tetanus toxin spreads in the body through the lymphatic and vascular systems to the neuromuscular junction, internalized to peripheral neuron synapses, and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons to the CNS5. There, it inhibits neurotransmitter release by the specific degradation of the vesicle-secretory protein-Synaptobrevin6.
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Electrophysiology: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
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