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Chlorotoxin

ALX-630-069

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Cl^– channel blocker

Potent neurotoxin. Small conductance Cl^– channel blocker. Highly specific marker for glioma cells and tumors of neuroectodermal origin. Inhibits the activity of matrix metalloproteinase-2 (MMP-2).

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Product Details

Appearance	Lyophilized.
CAS	163515-35-3
Formula	C₁₅₈H₂₄₉N₅₃O₄₇S₁₁
MW	3995.8
Purity	≥98% (TLC, HPLC)
Quantity	Vial contains exactly 0.55mg (0.14µmol)
Reconstitution	Reconstitute by injecting 1.4ml of distilled water into the vial using a calibrated syringe. Then dissolve the contents thoroughly to receive a 10-4 M solution.
Sequence	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-Pro-Gln-Cys-Leu-Cys-Arg-NH₂ (Disulfide bonds between Cys²-Cys¹⁹, Cys⁵-Cys²⁸, Cys¹⁶-Cys³³and Cys²⁰-Cys³⁵)
Solubility	Soluble in water
Source	Synthetic.

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended. Aliquots are stable for a few weeks when stored at -20°C.
Handling	After reconstitution, prepare aliquots and store at -20°C.
Long Term Storage	-20°C
Shipping	Ambient Temperature

Regulatory Status	RUO – Research Use Only

Targeted delivery of antitumoral therapy to glioma and other malignancies with synthetic chlorotoxin (TM-601): A. N. Mamelak & D. B. Jacoby; Expert Opin. Drug Deliv. 4, 175 (2007), (Review), Abstract
Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2: J. Deshane, et al.; J. Biol. Chem. 278, 4135 (2003), Abstract
Chlorotoxin, a scorpion-derived peptide, specifically binds to gliomas and tumors of neuroectodermal origin: S.A. Lyons, et al.; Glia 39, 162 (2002), Abstract
Use of chlorotoxin for targeting of primary brain tumors: L. Soroceanu, et al.; Cancer Res. 58, 4871 (1998), Abstract
NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels: G. Lippens, et al.; Biochemistry 34, 13 (1995), Abstract
Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion: J.A. DeBin, et al.; Am. J. Physiol. 264, C361 (1993), Abstract