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M7444
Maurotoxin
recombinant, expressed in E. coli, ≥95% (HPLC), lyophilized powder
Synonym(e):
MTX scorpion toxin
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About This Item
Rekombinant
expressed in E. coli
Qualitätsniveau
Assay
≥95% (HPLC)
Form
lyophilized powder
Mol-Gew.
3613
Versandbedingung
wet ice
Lagertemp.
−20°C
Amino Acid Sequence
Val-Ser-Cys-Thr-Gly-Ser-Lys-Asp-Cys-Tyr-Ala-Pro-Cys-Arg-Lys-Gln-Thr-Gly-Cys-Pro-Asn-Ala-Lys-Cys-Ile-Asn-Lys-Ser-Cys-Lys-Cys-Tyr-Gly-Cys
Biochem./physiol. Wirkung
Maurotoxin is a 34 amino acid recombinant toxin, originally isolated from the venom of the scorpion Scorpio Maurus palmatus; a member of the α-KTx6.2 scorpion toxin family. It blocks voltage-gated potassium channels (KV1.1/KCNA1, KV1.2/KCNA2, and KV1.3/KCNA3) and inhibits apamin-sensitive small conductance calcium-activated channels (SK channels), particularly KCa3.1(IKca1, SK4).
Leistungsmerkmale und Vorteile
This compound is featured on the Potassium Channels page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
Rekonstituierung
Stock solution of 1 μm can be obtained by adding 0.277 mL of any conventional buffer per μg of protein.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Analysenzertifikate (COA)
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N A Castle et al.
Molecular pharmacology, 63(2), 409-418 (2003-01-16)
Maurotoxin, a 34-amino acid toxin from Scorpio maurus scorpion venom, was examined for its ability to inhibit cloned human SK (SK1, SK2, and SK3), IK1, and Slo1 calcium-activated potassium (K(Ca)) channels. Maurotoxin was found to produce a potent inhibition of
Violeta Visan et al.
Molecular pharmacology, 66(5), 1103-1112 (2004-08-03)
Maurotoxin (MTX) is a potent blocker of human voltage-activated Kv1.2 and intermediate-conductance calcium-activated potassium channels, hIKCa1. Because its blocking affinity on both channels is similar, although the pore region of these channels show only few conserved amino acids, we aimed
Ricardo C Rodríguez de la Vega et al.
Toxicon : official journal of the International Society on Toxinology, 43(8), 865-875 (2004-06-23)
Much of our knowledge on K+-channels was elucidated using specific peptide ligands isolated from a number of venomous organisms. Recently, this field received a strong support and increased interest due to the solution of the three-dimensional structure of a couple
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