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Application
Dendrotoxin-K is suitable for use as a potassium voltage-gated channel subfamily A member 1 (Kv1.1) channel blocker in axon and human embryonic kidney (HEK293) cells. It has also been used as a selective blocker of Kv channels in mice.
Biochem/physiol Actions
Dendrotoxin-K (DTXk) is isolated from mamba snake Dendroaspis polylepis and interacts with the β-turn region in the N-terminal sequence of the potassium channel. It inhibits tumor progression in gefitinib-resistant non-small cell lung cancer cells. DTXk induces neuronal damage in the hippocampus via N-methyl-d-aspartate (NMDA) and non-NMDA receptors.
Dendrotoxin-K inhibits potassium channels that contain Kv1.1 protein only.
Features and Benefits
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.
Other Notes
Isolated initially from Dendroaspis polylepis polylepis venom
Preparation Note
Purified by a modification of the method of Schweitz.
Reconstitution
Reconstitute in 1 mL deionized water or buffer (pH 7.5) to yield 10 μM stock
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Identification of residues in dendrotoxin K responsible for its discrimination between neuronal K+ channels containing Kv1. 1 and 1.2 alpha subunits
Wang FC, et al.
European Journal of Biochemistry, 263(1), 222-229 (1999)
Cav1. 3 calcium channels are required for normal development of the auditory brainstem
Hirtz JJ, et al.
The Journal of Neuroscience, 31(22), 8280-8294 (2011)
Effects of voltage-gated K+ channel blockers in gefitinib-resistant H460 non-small cell lung cancer cells
Jeon WIL, et al.
Anticancer Research, 32(12), 5279-5284 (2012)
H Schweitz et al.
Toxicon : official journal of the International Society on Toxinology, 28(7), 847-856 (1990-01-01)
This paper reports the purification of 28 different peptides from the venom of the snake Dendroaspis polylepis. These peptides represent 99% of the total peptide fraction in the venom. The 14 most cationic peptides form a structurally and functionally homogeneous
F C Wang et al.
European journal of biochemistry, 263(1), 222-229 (1999-08-03)
Dendrotoxin (DTX) homologues are powerful blockers of K+ channels that contain certain subfamily Kv1 (1.1-1.6) alpha- and beta-subunits, in (alpha)4(beta)4 stoichiometry. DTXk inhibits potently Kv1.1-containing channels only, whereas alphaDTX is less discriminating, but exhibits highest affinity for Kv1.2. Herein, the
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