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Chlorotoxin

Cl- channel blocker
 
ALX-630-069-C500 500 µg 1,187.00 USD
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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).

Product Details

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)
 
Formula:C158H249N52O48S11
 
MW:3995.8
 
Source:Synthetic.
 
CAS:163515-35-3
 
Quantity:Vial contains exactly 0.55mg (0.14µmol)
 
Purity:≥98% (TLC, HPLC)
 
Appearance:Lyophilized.
 
Solubility:Soluble in water
 
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.
 
Shipping:Ambient Temperature
 
Long Term Storage:-20°C
 
Use/Stability:Aliquots are stable for a few weeks when stored at -20°C.
 
Handling:After reconstitution, prepare aliquots and store at -20°C.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

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;

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