Tertiapin Q: toxin properties
Tertiapin has been isolated from the venom of the Honeybee Apis mellifera (African tarantula) tertiapin-Q is a mutant of tertiapin where M13 has been mutated by Q in order to increase your stability. This is a neurotoxin with presynaptic activity that blocks the inwardly rectifying Kir1.1 (KCNJ1) and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA/KCNMB) potassium channels in a concentration, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimer potassium channels. It can prevent dose-dependent acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh)), are activated by ACh found in mammalian myocytes. This toxin interacts specifically with calmodulin in the presence of calcium.
Product Specifications
AA sequence: H-Ala-Leu-Cys3-Asn-Cys5-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys14-Trp-Lys-Lys-Cys18-Gly-Lys-Lys-NH2
(Disulfide bonds between Cys3-Cys14 and Cys5-Cys18)
Length (aa): 21
Formula: C106H175N35O24S4
Molecular Weight: 2453.39 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: [252198-49;5]
Source: Synthetic
Purity rate: > 97 %
Price & Quantities
- 100 µg : 100 €
- 500 µg : 250 €
- 1 mg : 425 €
Other quantities available upon request
References
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Felix, J. P., Liu, J., Schmalhofer, W. A., Bailey, T., Bednarek, M. A., Kinkel, S., Weinglass, A. B., Kohler, M., Kaczorowski, G. J., Priest, B. T., and Garcia, M. L. (2006) Characterization of Kir1.1 channels with the use of a radiolabeled derivative of tertiapin, Biochemistry 45, 10129-10139.
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Kanjhan, R., Coulson, E. J., Adams, D. J., and Bellingham, M. C. (2005) Tertiapin-Q blocks recombinant and native large conductance K+ channels in a use-dependent manner, J Pharmacol Exp Ther 314, 1353-1361.
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Ramu, Y., Klem, A. M., and Lu, Z. (2001) Titration of tertiapin-Q inhibition of ROMK1 channels by extracellular protons, Biochemistry 40, 3601-3605.
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Kitamura, H., Yokoyama, M., Akita, H., Matsushita, K., Kurachi, Y., and Yamada, M. (2000) Tertiapin potently and selectively blocks muscarinic K(+) channels in rabbit cardiac myocytes, J Pharmacol Exp Ther 293, 196-205.
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Jin, W., Klem, A. M., Lewis, J. H., and Lu, Z. (1999) Mechanisms of inward-rectifier K+ channel inhibition by tertiapin-Q, Biochemistry 38, 14294-14301.
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Jin, W., and Lu, Z. (1999) Synthesis of a stable form of tertiapin: a high-affinity inhibitor for inward-rectifier K+ channels, Biochemistry 38, 14286-14293.