GsMTx4

Description

GsMTx4 has been isolated from the venom of the spider Grammostola rosea. This cationic hydrophobic polypeptide blocks mechanosensitive ion channels (also named strech-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. This Toxin acts by perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. Also it affects the membrane motor of outer hair cells at low doses. It does not inhibit the potassium channel KvAP (from the archaeon Aeropyrum pernix).

Product Specifications

AA sequence: H-Gly-Cys²-Leu-Glu-Phe-Trp-Trp-Lys-Cys⁹-Asn-Pro-Asn-Asp-Asp-Lys-Cys¹⁶-Cys¹⁷-Arg-Pro-Lys-Leu-Lys-Cys²³-Ser-Lys-Leu-Phe-Lys-Leu-Cys³⁰-Asn-Phe-Ser-Phe-NH₂
(Disulfide bonds between Cys²-Cys¹⁷, Cys⁹-Cys²³ and Cys¹⁶-Cys³⁰)
Length (AA): 34
Formula: C₁₈₅H₂₇₃N₄₉O₄₅S₆
Molecular Weight: 4095.2 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number:
Source: Synthetic
Purity rate: > 97 %

Price & Quantities

• 50 µg : 100 €
• 100µg : 180 €
• 500 µg : 450 €

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References

• Bae, C.,  et al. The Mechanosensitive Ion Channel Piezo1 Is Inhibited by the Peptide GsMTx4. Biochemistry, 2011, 50 (29), pp 6295–6300. PubMed link
• Ruta, V., and MacKinnon, R. (2004) Localization of the voltage-sensor toxin receptor on KvAP, Biochemistry 43, 10071-10079. PubMed link
• Ostrow, K. L., et al. (2003) cDNA sequence and in vitro folding of GsMTx4, a specific peptide inhibitor of mechanosensitive channels, Toxicon 42, 263-274. PubMed link
• Oswald, R. E., et al. (2002) Solution structure of peptide toxins that block mechanosensitive ion channels, J Biol Chem 277, 34443-34450. PubMed link
• Suchyna, T. M., et al. (2000) Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels, J Gen Physiol 115, 583-598. PubMed link

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