M7444
Maurotoxin
recombinant, expressed in E. coli, ≥95% (HPLC), lyophilized powder
Sinônimo(s):
MTX scorpion toxin
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About This Item
recombinante
expressed in E. coli
Nível de qualidade
Ensaio
≥95% (HPLC)
forma
lyophilized powder
peso molecular
3613
Condições de expedição
wet ice
temperatura de armazenamento
−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
Ações bioquímicas/fisiológicas
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).
Características e benefícios
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.
Reconstituição
Stock solution of 1 μm can be obtained by adding 0.277 mL of any conventional buffer per μg of protein.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
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Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
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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