

| 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
|
| Expression system | E. coli |
| Accession | O43526 |
| Protein length | Thr368-Gly596 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo 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 Names | KCNQ2, 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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