Potassium voltage-gated channel subfamily H member 2 (KCNH2, ERG, ERG1, HERG truncated)
Description
Introducing our off-the-shelf, full-length, active, and native Potassium Voltage-Gated Channel Subfamily H Member 2, also known as KCNH2, ERG, ERG1, and hERG. This voltage-dependent potassium channel is crucial for the repolarization of the cardiac action potential, making it an essential target in cardiovascular research.
hERG is an important anti-drug target, known to interact with various drugs leading to acquired long QT syndrome, which can precede the onset of life-threatening arrhythmias.
Our hERG protein has been solubilized and stabilized using Cube Biotech's NativeMP™ Platform, ensuring it retains its native structure and full biological activity, making it ideal for a wide range of research applications.
Applications:
- Screening/Validation
- Biologics Development
- Structure Determination
- Small Molecule Drug Development
The protein delivered can be used for these specific applications. When ordering, please indicate which applications you intend to use the protein for in the contact form to ensure the best results.
For more details, explore our solubilization database.
Datasheets
| Feature | |
|---|---|
| Alternative names | KCNH2, ERG, ERG1, HERG |
| UniProt Number | Q12809 |
| Protein class | Ion channel |
| Original host | Homo sapiens |
| Sequence, One-Letter Code | MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSSPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGGRQYQELPRCPAPTPSLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGSDPGSLEVLFQGPGSSGTETSQVAPA |
| Affinity tags | HRV3C cleavage site, Rho1D4-tag (C-terminal) |
| Deletions | Δ141-350, Δ871-1005 |
| Size (excluding additional elements) | 835 amino acids, 93 kDa |
| Concentration | 0,4 - 0,7 mg/ml |
| Purity | >90%, determined via SDS-PAGE |
| Purification process | 2-step purification |
| Shipping | Shipment is carried out on dry-ice for temperature stability to ensure the integrity of the product. |
| Function | Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (PubMed:18559421, PubMed:26363003, PubMed:27916661). {ECO:0000269|PubMed:18559421, ECO:0000269|PubMed:26363003, ECO:0000269|PubMed:27916661}.; [Isoform A-USO]: Has no channel activity by itself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation. {ECO:0000269|PubMed:18559421}.; [Isoform B-USO]: Has no channel activity by itself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation. {ECO:0000269|PubMed:18559421}. |
| PubMed ID | 8159766, 9600240, 11374908, 12431979, 18559421, 19412172, 12853948, 9351462, 9351446, 10790218, 15489334, 9765245, 12063277, 10837251, 9230439, 10219239, 16361248, 19690332, 23186163, 25281747, 26363003, 27916661, 9845367, 7889573, 8914737, 8635257, 8877771, 9024139, 9693036, 9544837, 9452080, 10086971, 10220144, 10187793, 10517660, 10735633, 10973849, 10862094, 10753933, 11170080, 12062363, 11997281, 12442276, 12354768, 12621127, 14676148, 15051636, 15840476, 16414944, 15828882, 16922724, 19716085, 22314138 |
Lab Results
