| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | M-TRTx-Gr1a, M-theraphotoxin-Gr1a, GsMTx4, TRPC1, TRPC6, Piezo1 |
| Concentration | |
| Conjugate | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| 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 pure water at high-micromolar concentrations (50 µM - 1 mM). For long-term storage in solution, it is recommended to prepare 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 at 10,000 x g for 5 minutes 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 | Modified synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
GsMTx-4-Biotin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to NaV1.7 channels, TRPC1, TRPC6, Piezo1 biology and/or assay development. The reagent is provided as a Biotin conjugate, supporting detection or imaging workflows where applicable. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology, Live cell imaging, Immunofluorescence, Fluorescence staining, Indirect flow cytometry.
Key elements and design rationale
- Molecular identity: MW: 4435 Da.
- Source / origin: Grammostola rosea (Chilean rose) tarantula.
- Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys2-Cys17, Cys9-Cys23, and Cys16-Cys30 Phe34 - C-terminal amidationLC-Biotin
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
GsMTx-4 is a 34 amino acid peptidyl toxin originally isolated from the Grammostola rosea (Chilean rose) tarantula venom and belongs to the huwentoxin-1 family1. This toxin inhibits different channels and in addition has antimicrobial activity. It blocks cation-selective mechanosensitive ion channels (strech-activated channels, SACs), without having an effect on whole-cell voltage-sensitive currents1. In addition, it inhibits atrial fibrillation2 as well as the membrane motor of outer hair cells3 at low doses. A medium toxicity on a large spectra of voltage-gated Na+ channels, namely NaV1.1, NaV1.2, NaV1.3, NaV1.4, NaV1.5, NaV1.6 and NaV1.7 was reported. GsMTx-4 also inhibits K+ channels KV11.1 and KV11.2, whereas it does not inhibit K+ channels KV1.1 (IC50 > 85 µM), KV1.4 (IC50 > 85 µM) and KV11.3 (IC50 = 53 µM)4. GsMTx-4 was also found to inhibit both TRPC1 and TRPC6 channels5,6, as well as Piezo1, the mechanosensitive channel7. Antimicrobial activity is shown against several Gram-positive and Gram-negative bacteria as well8.
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.
- Live cell imaging: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Immunofluorescence: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Fluorescence staining: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Indirect flow cytometry: 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.
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Redaelli, E.
et al. (2010) J. Biol. Chem. 285, 4130.
Suchyna, T.M.
et al. (2000) J. Gen. Physiol.115, 583.
Bode, F.
et al. (2001) Nature409, 35.
Fang, J. and Iwasa, K.H.
(2006) Neurosci. Lett.404, 213.
Redaelli, E.
et al. (2010) J. Biol. Chem.285, 4130.
Spassova, M.A.
et al. (2006) Proc. Natl. Acad. Sci.U.S.A.103, 16586.
Alessandri-Haber, N.
et al. (2009) J. Neurosci.29, 6217.
Ostrow, K.L.
et al. (2003) Toxicon 42, 263.
Bae, C.
et al. (2011) Biochemistry 50, 6295.
Ostrow, K.L.
et al. (2003) Toxicon 42, 263.
Suchyna, T.M.
et al. (2000) J. Gen. Physiol. 115, 583.
