Chlorotoxin is a chloride channel blocker which has been found in the venom of the Egyptian scorpion Leiurus quinquestriatus. The toxin has recently been reported to specifically bind to a protein complex on the surface of glioma cells containing several proteins implicated in glioma cell invasion and thus inhibit their invasive potential. Gelatinase A (matrix metalloproteinase-2 (MMP2)) is one of the components present in this complex. The anti-invasive effect of chlorotoxin seems to be mediated by binding to and direct inhibition of gelatinase A, and its surface down-regulation. Chlorotoxin is available in bulk quantities, produced according to cGMP. References:
Properties for From Egyptian scorpion: [Cys2-Cys19, Cys5-Cys28, Cys16-Cys33, Cys20-Cys35] H-Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-His-Gln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-Cys-Gly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-Gly-P
Molecular Weight:
4004.76 g·mol−1
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Alternative Distributors of [From Egyptian scorpion: [Cys2-Cys19, Cys5-Cys28, Cys16-Cys33, Cys20-Cys35] H-Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-His-Gln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-Cys-Gly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-Gly-P]
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