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Human KCNK3 Recombinant Protein (N-His) (HT022012)

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Overview
Catalog No.HT022012
Description
Recombinant Human KCNK3 Protein, N-His (HT022012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionO14649
Protein lengthLeu244-Val394
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesAcid-sensitive potassium channel protein TASK-1, KCNK3, Potassium channel subfamily K member 3, TASK, TASK1, TWIK-related acid-sensitive K(+) channel 1, Two pore K(+) channel KT3.1, Two pore potassium channel KT3.1
Background

Potassium channel subfamily K member 3 is a ~43 kDa protein. K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Changes ion selectivity and becomes permeable to Na(+) ions in response to extracellular acidification. Protonation of the pH sensor His-98 stabilizes C-type inactivation conformation likely converting the channel from outward K(+)-conducting, to inward Na(+)-conducting to nonconductive state. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties.

1. Plant, LD. et al. (2012) Science signaling 5, ra84. PMID: 23169818
2. Schewe, M. et al. (2016) Cell 164, 937-49. PMID: 26919430
3. Rödström, KEJ. et al. (2020) Nature 582, 443-447. PMID: 32499642
4. Sörmann, J. et al. (2022) Nature genetics 54, 1534-1543. PMID: 36195757
5. Duprat, F. et al. (1997) The EMBO journal 16, 5464-71. PMID: 9312005
6. Ma, L. et al. (2012) The Journal of biological chemistry 287, 37145-53. PMID: 22948150
Note For research use only
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Formula
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Formula
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