Recombinant Human Potassium Voltage-Gated Channel Subfamily E Member 2 (KCNE2) Protein (His)

Name: Recombinant Human Potassium Voltage-Gated Channel Subfamily E Member 2 (KCNE2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01159P
Price: 2879.2 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Potassium Voltage-Gated Channel Subfamily E Member 2 (KCNE2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y6J6
Target Symbol	KCNE2
Synonyms	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)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVILYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQILNLEESKATIHENIGAAGFKMSP
Expression Range	1-123aa
Protein Length	Full Length
Mol. Weight	17.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Protein Families	Potassium channel KCNE family
Database References	HGNC: 6242 OMIM: 603796 KEGG: hsa:9992 STRING: 9606.ENSP00000290310 UniGene: Hs.551521
Associated Diseases	Long QT syndrome 6 (LQT6); Atrial fibrillation, familial, 4 (ATFB4)
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

Gene Functions References

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
These results demonstrate that KCNE2 is required for normal beta-cell electrical activity and insulin secretion, and that Kcne2 deletion causes T2DM. PMID: 28280005
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
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
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
M54T MiRP1 mutation axecerbate drug-induced long QT syndrome and arrhythmia. PMID: 24631769
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
Mutations in KCNE2 has been shown to cause familial atrial fibrillation. PMID: 24460807
The transmembrane domains (TMDs) of KCNE1 and KCNE2 were illustrated to associate with the KCNQ1 channel in different modes. PMID: 24827085
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
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
Case Report: reduced expression of KCNE2 in surgically excised tissue from human gastric cancer associated with gastritis cystica profunda. PMID: 23483772
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
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
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
Backbone assignments of most MiRP1 residues were achieved through a series of triple resonance NMR experiments. PMID: 21087668
Results suggest KCNE2 disruption as a possible risk factor for gastric neoplasia. PMID: 20625512
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
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
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
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
KCNE2 protein is expressed in ventricles, and it can play diverse roles in ventricular electrical activity under (patho)physiological conditions. PMID: 15066947
KCNE2 R27C is a gain-of-function mutation associated with the initiation and/or maintenance of Atrial Fibrillation. PMID: 15368194
These results suggest that KCNE2 can functionally couple to KCNQ1 even in the presence of KCNE1. PMID: 16631607
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
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
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
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
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
KChIP2c and KCNE2 simultaneously participate in recapitulation of the electrophysiological properties of transient outward current in cardiac myocytes PMID: 18501111
KCNE variants reveal a critical role of the beta subunit carboxyl terminus in PKA-dependent regulation of the IKs potassium channel, KCNQ1. PMID: 19077539
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
in cardiac myocytes the IKs current amplitude is under dynamic control by the availability of KCNE2 subunits in the cell membrane PMID: 19372218
Observational study of genotype prevalence and genetic testing. (HuGE Navigator) PMID: 16414944
Observational study of genetic testing. (HuGE Navigator) PMID: 16487842

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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