AA sequence: Arg-Pro-Thr-Asp-Ile-Lys-Cys7-Ser-Glu-Ser-Tyr-Gln-Cys13-Phe-Pro-Val-Cys17-Lys-Ser-Arg-Phe-Gly-Lys-Thr-Asn-Gly-Arg-Cys28-Val-Asn-Gly-Phe-Cys33-Asp-Cys35-Phe-OH
Disulfide bonds: Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35
Length (aa): 36
Formula: C174H261N51O52S6
Molecular Weight: 4091.70 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: Not available
Source: Synthetic
Purity rate: > 97%
BeKm-1
135 $ – 390 $
Selective blocker of ERG1 channel
BeKm-1 toxin is a peptide toxin that has been isolated from the venom of the Central Asian scorpion Buthus eupeus. BeKm-1 toxin has been reported to be a highly selective inhibitor of the human ether-a-go-go ERG1 channel (hERG1). BeKm-1 inhibits hERG1 channels expressed in HEK-293 cells with an IC50 of 3.3 nM, but has no effect at 100 nM on human EAG, human SK1, rat SK2, human IK, human BK, KCNQ1/KCNE1, KCNQ2/KCNQ3, and KCNQ4 channels. It has also minimal effects on rat ELK1 channel. BeKm-1 inhibits the human ERG1 + KCNE1 combination transiently expressed in HEK-293 cells with an IC50 value in the range of 10 to 30 nM. BeKm-1 toxin preferentially blocks human ERG channel through the closed (resting) state, although some open channel blockade is also reported to occur.
Interaction simulation of hERG K+ channel with its specific BeKm-1 peptide: insights into the selectivity of molecular recognition.
Yi H., et al. (2007) Interaction simulation of hERG K+ channel with its specific BeKm-1 peptide: insights into the selectivity of molecular recognition. J Proteome Res. PMID 17269718
BeKm-1, a peptide inhibitor of human ether-a-go-go-related gene potassium currents, prolongs QTc intervals in isolated rabbit heart.
Qu Y., et al. (2011) BeKm-1, a peptide inhibitor of human ether-a-go-go-related gene potassium currents, prolongs QTc intervals in isolated rabbit heart. J Pharmacol Exp Ther. PMID 21205913
Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin.
Milnes J., et al. (2003) Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin. FEBS Letters. PMID12860380
New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1.
Korolkova Y., et al. (2002) New Binding Site on Common Molecular Scaffold Provides HERG Channel Specificity of Scorpion Toxin BeKm-1. JBC. PMID:12151390
An ERG channel inhibitor from the scorpion Buthus eupeus.
Korolkova Y., et al. (2001) An ERG Channel Inhibitor from the Scorpion Buthus eupeus. JBC. PMID:11136720