Recombinant Human Potassium voltage-gated channel subfamily E member 2(KCNE2)-VLPs

Code CSB-MP896548HU(A4)
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Product Details

Target Names KCNE2
Uniprot No. Q9Y6J6
Research Area Others
Alternative Names KCNE2; Potassium voltage-gated channel subfamily E member 2; MinK-related peptide 1; Minimum potassium ion channel-related peptide 1; Potassium channel subunit beta MiRP1
Species Homo sapiens (Human)
Source Mammalian cell
Expression Region 1-123aa
Target Protein Sequence MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVILYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQILNLEESKATIHENIGAAGFKMSP
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info C-terminal 10xHis-tagged
If you have specified tag type, please tell us and we will check if it’s possible to develop.
Form Lyophilized powder
Note: We will default ship it in lyophilized form with normal bule ice packs. However, if you request to ship in liquid form, it needs to be shipped with dry ice, please communicate with us in advance and extra fees for dry ice and dry ice box will be charged.
Buffer Lyophilized from PBS, 6% Trehalose, pH 7.4
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store the protein at -20°C/-80°C upon receiving it, and ensure to avoid repeated freezing and thawing, otherwise, it will affect the protein activity.
Datasheet & COA Please contact us to get it.

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Target Background

Function
Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current. Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current.
Gene References into Functions
  1. On the basis of clinical phenotype, the high allelic frequencies of LQT6 mutations in the Exome Aggregation Consortium database, and absence of previous documentation of genotype-phenotype segregation, our findings suggest that many KCNE2 variants, and perhaps all, have been erroneously designated as LQTS-causative mutations. Instead, KCNE2 variants may confer proarrhythmic susceptibility when provoked by additional envir PMID: 28794082
  2. These results demonstrate that KCNE2 is required for normal beta-cell electrical activity and insulin secretion, and that Kcne2 deletion causes T2DM. PMID: 28280005
  3. The identification of Filamin C as a novel KCNE2 ligand not only enhances current understanding of ion channel function and regulation, but also provides valuable information about possible pathways likely to be involved in long-QT syndrome pathogenesis PMID: 26956495
  4. KCNE2 has been widely studied since its role in the heart was discovered; it is association with inherited and acquired human Long QT syndrome; physiological analyses together with genetics studies have uncovered a startling array of functions for KCNE2, in the heart, stomach, thyroid and choroid plexus. [Review] PMID: 26123744
  5. Women with elevated BMI have enhanced hERG activity as a result of low beta-inhibitory protein expression, which likely contributes to weak contractions and poor labour outcomes. PMID: 24937480
  6. M54T MiRP1 mutation axecerbate drug-induced long QT syndrome and arrhythmia. PMID: 24631769
  7. The effect of KCNE2 mutations on KV7.1 was abolished in the presence of the major IKs beta-subunit KCNE1, when coexpressed in a 1:1:1 molar ratio. PMID: 24796621
  8. Mutations in KCNE2 has been shown to cause familial atrial fibrillation. PMID: 24460807
  9. The transmembrane domains (TMDs) of KCNE1 and KCNE2 were illustrated to associate with the KCNQ1 channel in different modes. PMID: 24827085
  10. study concluded that the variants in KCNQ1, KCNH2, KCNE1 and KCNE2 genes may be correlated with the occurrence of part of sudden unexplained nocturnal death syndrome cases in southern China PMID: 23890619
  11. Subjects with LQT-PM may have longer QTc intervals at rest and at peak exercise and all phases of the recovery period compared to controls. Those with homozygous SNPs (KCNE2 1%) had longer resting QTc intervals when compared to heterozygotes. PMID: 23714088
  12. Case Report: reduced expression of KCNE2 in surgically excised tissue from human gastric cancer associated with gastritis cystica profunda. PMID: 23483772
  13. KCNE1 and KCNE2, auxiliary subunits of voltage-gated potassium channels, undergo sequential cleavage mediated by either alpha-secretase and presenilin(PS)/gamma-secretase or BACE1 and PS/gamma-secretase in cells. PMID: 23504710
  14. The known interactions of the KCNE2 protein and the resulting functional effects, the effects of mutations in KCNE2 and their clinical role are discussed. [review] PMID: 22166675
  15. KCNE2 can modulate its partner channel function not only by altering channel conductance and/or gating kinetics, but also by affecting protein stability. PMID: 22180649
  16. Backbone assignments of most MiRP1 residues were achieved through a series of triple resonance NMR experiments. PMID: 21087668
  17. Results suggest KCNE2 disruption as a possible risk factor for gastric neoplasia. PMID: 20625512
  18. KCNE2 plays a role in normal function of native I(to) channel complex in human heart, M54T and I57T variants lead to gain of function of I(to), contributing to generating potential arrhythmogeneity and pathogenesis for inherited fatal rhythm disorders. PMID: 20042375
  19. The accelerated inactivation time course of HERG/MiRP1(V65M) channels may decrease I(Kr) current density of myocardial cells, thereby impairing the ability of myocytes to repolarize in response to sudden membrane depolarizations such as extrasystoles. PMID: 12185453
  20. KCNE2, by modulating I(f) or I(h) currents, might thus contribute to the electrophysiological diversity of known pacemaking currents in the heart and brain PMID: 12856183
  21. Most significant effects of MiRP1 subunits on HERG channels were more negative steady-state activation for HERG + T8A MiRP1 and more positive steady-state activation for HERG + M54T MiRP1 compared to either HERG + WT MiRP1 or HERG alone. PMID: 12923204
  22. KCNE2 protein is expressed in ventricles, and it can play diverse roles in ventricular electrical activity under (patho)physiological conditions. PMID: 15066947
  23. KCNE2 R27C is a gain-of-function mutation associated with the initiation and/or maintenance of Atrial Fibrillation. PMID: 15368194
  24. These results suggest that KCNE2 can functionally couple to KCNQ1 even in the presence of KCNE1. PMID: 16631607
  25. We demonstrated that 9.5% of cases diagnosed as SIDS carry functionally significant genetic variants in LQTS genes (KCNQ1, KCNH2, SCN5A, KCNE1, KCNE2, KCNJ2, CAV3). PMID: 17210839
  26. External pH can modify current amplitude and biophysical properties of KCNQ1. KCNE subunits work as molecular switches by modulating the pH sensitivity of human KCNQ1. PMID: 17310097
  27. We propose that the KCNE2 TMD adopts an alpha-helical secondary structure with one face making intimate contact with the KCNQ1 pore domain, while the contacts with the KCNQ1 voltage-sensing domain appear more dynamic. PMID: 17676362
  28. Results suggest that during biogenesis of channels HERG is more likely to assemble with KCNE1 than KCNE2 due to distinctly different trafficking rates and retention in the cell rather than differences in relative affinity. PMID: 17895974
  29. results show that MiRP1 is largely alpha helical and that the predicted transmembrane and intracellular domains in particular require extensive hydrophobic interaction for adoption of ordered, non-aggeegated structure PMID: 18221016
  30. KChIP2c and KCNE2 simultaneously participate in recapitulation of the electrophysiological properties of transient outward current in cardiac myocytes PMID: 18501111
  31. KCNE variants reveal a critical role of the beta subunit carboxyl terminus in PKA-dependent regulation of the IKs potassium channel, KCNQ1. PMID: 19077539
  32. Human MiRP1 slowed Kv2.1 activation and deactivation twofold. Compared to wild-type human MiRP1-Kv2.1 complexes, channels formed with M54T- or I57T-MiRP1 showed greatly slowed activation (tenfold and fivefold, respectively). PMID: 19219384
  33. in cardiac myocytes the IKs current amplitude is under dynamic control by the availability of KCNE2 subunits in the cell membrane PMID: 19372218
  34. Observational study of genotype prevalence and genetic testing. (HuGE Navigator) PMID: 16414944
  35. Observational study of genetic testing. (HuGE Navigator) PMID: 16487842

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Involvement in disease Long QT syndrome 6 (LQT6); Atrial fibrillation, familial, 4 (ATFB4)
Subcellular Location Cell membrane; Single-pass type I membrane protein.
Protein Families Potassium channel KCNE family
Tissue Specificity Highly expressed in brain, heart, skeletal muscle, pancreas, placenta, kidney, colon and thymus. A small but significant expression is found in liver, ovary, testis, prostate, small intestine and leukocytes. Very low expression, nearly undetectable, in lu
Database Links

HGNC: 6242

OMIM: 603796

KEGG: hsa:9992

STRING: 9606.ENSP00000290310

UniGene: Hs.551521

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