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Human KCNQ2/Kv7.2 Recombinant Protein (N-His) (HT472012)

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Overview
Catalog No.HT472012
Description
Recombinant Human KCNQ2/Kv7.2 Protein, N-His (HT472012) expressed in E. coli, spanning Thr368-Gly596. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionO43526
Protein lengthThr368-Gly596
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.
Predicted molecular weight 27.37 kDa
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 NamesKCNQ2, KQT-like 2, Neuroblastoma-specific potassium channel subunit alpha KvLQT2, Potassium voltage-gated channel subfamily KQT member 2, Voltage-gated potassium channel subunit Kv7.2
Background

Potassium voltage-gated channel subfamily KQT member 2 is a ~95 kDa protein. Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability. M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers. The native M-current has a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2-KCNQ3 M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+).

1. Zhang, Q. et al. (2013) Proceedings of the National Academy of Sciences of the United States of America 110, 20093-8. PMID: 24277843
2. Manville, RW. et al. (2017) Biophysical journal 113, 613-626. PMID: 28793216
3. Wang, HS. et al. (1998) Science (New York, N.Y.) 282, 1890-3. PMID: 9836639
4. Cooper, EC. et al. (2000) Proceedings of the National Academy of Sciences of the United States of America 97, 4914-9. PMID: 10781098
5. Singh, NA. et al. (2003) Brain : a journal of neurology 126, 2726-37. PMID: 14534157
6. Li, X. et al. (2021) Cell research 31, 52-61. PMID: 32884139
7. Ma, D. et al. (2023) Nature communications 14, 6632. PMID: 37857637
Note For research use only
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