| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | µ-theraphotoxin-Tsp1a, Tsp1a, µ-TRTX-Tsp1a, Mu-TRTX-Tsp1a |
| 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. The product is soluble in pure water at high micromolar concentrations (100 µM - 1 mM). For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in double-distilled water (ddH2O) at a concentration between 100-1000x of the final working concentration. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. Centrifuge all product preparations before use. It is recommended to prepare fresh solutions in working buffers just before use. Avoid multiple freeze-thaw cycles to maintain biological activity. |
| Source | Synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
µ-TRTX-Tsp1a is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to Nav 1.7 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.
Key elements and design rationale
- Molecular identity: MW: 3391 Da, Formula: C148H221N41O39S6.
- Source / origin: Thrixopelma spec. (Peru) spider.
- Quality attributes: Purity: ≥97% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys2-Cys16, Cys9-Cys21, Cys15-Cys28 Asn28 - C-terminal amidation
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
μ-theraphotoxin-Tsp1a (Tsp1a) is a 28 amino acid peptidyl toxin originally isolated from the venom of the Thrixopelma spec. (Peru) spider venoM Tsp1a is a potent (IC50 = 10 nM) and highly specific inhibitor of NaV1.7 channels, with a selectivity of >100-fold over hNaV1.3−hNaV1.6 and hNaV1.8, 45-fold over hNaV1.1, and 24-fold over hNaV1.21.Tsp1a is a gating modifier toxin that inhibits hNaV1.7 by stabilizing the channel in its inactivated state, inducing a hyperpolarizing shift in the voltage-dependence of channel inactivation and slowing recovery from fast inactivation1.Spider peptides modulate an array of ion channels and receptor proteins. Knottins, which are a subtype of spider peptides, are also referred to as inhibitor cystine knot (ICK) peptides. ICK peptides harbor a disulfide-rich structural motif that forms a "knot", which confers high structural, thermal, and proteolytic stability. NMR studies revealed that Tsp1a adopts a classical knottin fold, and like many knottin peptides, it is exceptionally stable in human serum1.NaV1.7 is expressed in the PNS, dorsal root ganglia neurons, visceral sensory neurons, olfactory sensory neurons, trigeminal ganglia, and sympathetic neurons. Gain-of-function mutations in SCN9A, the gene encoding NaV1.7, have been identified in patients with various pain disorders, such as inherited erythromelalgia (IEM), paroxysmal extreme pain disorder (PEPD), small fiber neuropathy (SFN), and painful diabetic peripheral neuropathy. Nav 1.7 loss-of-function mutations lead to a congenital indifference to pain2,3. Tsp1a toxin was shown to reduce visceral hypersensitivity in a model of irritable bowel syndrome. This suggests that pharmacological inhibition of hNaV1.7 at peripheral sensory nerve endings might be a viable approach for eliciting analgesia in patients suffering from chronic visceral pain1.
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.
- 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.
Pedarzani, P.
et al. (2002) J. Biol. Chem. 277, 46101.
Jiang, Y.
et al. (2021) ACS Pharmacol. Transl. Sci., 4, 1362.
Dongol, Y
. et al. (2019) Toxins 11, 626.
Dib-Hajj, S.D.
et al. (2007) Trends Neurosci., 30, 555.
