| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | α-Latrotoxin-Lt1a, α-LTX-Lt1a, α-LTX, ADGRL1 (latrophilin-1/CIRL), tyrosine-protein phosphatase S (PTPRS) receptors |
| 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) to spin down all the powder to the bottom of the vial. The lyophilized product 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 water. Once dissolved in water, add an equal volume of glycerol. Do not shake or vortex. Avoid multiple freeze-thawing cycles. |
| Source | Natural protein |
| Species | |
| Storage | |
| Target |
Overview
α-Latrotoxin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to Neurexin-1, ADGRL1 (latrophilin-1/CIRL), and tyrosine-protein phosphatase S (PTPRS) receptors biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology, Synaptic recording.
Key elements and design rationale
- Molecular identity: CAS: 65988-34-3, MW: 130 kDa.
- Source / origin: Latrodectus tredecimguttatus (Mediterranean black widow spider)..
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.
Modifications
Highly disulfide bridged protein Glycosylated
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
α-Latrotoxin is a 130 kDa protein toxin from the black widow spider venom and is the only protein in the venom that affects mammals.1,2 Application of the toxin to presynaptic preparations induces, after a delay, a huge increase in spontaneous neurotransmitter release, which can be evaluated by measuring the post synaptic response in the form of miniature end plate potentials. This toxin is widely used to induce and study neurotransmitter release, but the molecular mechanism of its action is not fully determined.α-Latrotoxin is isolated according to a modified protocol as described by Frontali3 and Grasso4.
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.
- Synaptic recording: 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.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- 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.
Ushkaryov, Y.
et al. (2002) Toxicon 40, 1.
Frontali, B.
et al. (1976) J. Cell Biol. 68, 462.
Grasso, A.
et al. (1976) Biochim. Biophys. Acta. 439, 406.
Grasso, A.
et al. (1976) Biochim. Biophys. Acta. 439, 406.
Sudhof, T.C.
et al. (2001) Annu. Rev. Neurosci. 24, 933.
Frontali, N.
et al. (1976) J. Cell Biol. 68, 462.
