|Application ||WB, IP|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||14356 Da|
|Homology||Mouse - 18/20 amino acid residues identical; human - 16/20 amino acid residues identical; rabbit - 15/20 amino acid residues identical.|
|Other Names||Potassium voltage-gated channel subfamily E member 2, MinK-related peptide 1, Minimum potassium ion channel-related peptide 1, Potassium channel subunit beta MiRP1, Kcne2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)IVEDWQQKYRSQILHLEDSK, corresponding to amino acid residues 88-107 of rat KCNE2 (MiRP1) (Accession P63161).ֲ ֲ Intracellular, C-terminal part.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Application Details||Western blot analysis (WB): - Cultured mouse primary cortical/hippocampal neurons (1:250) (see Sachse, C.C. et al. in Product Citations). - Human ventricle lysate (see Zhang, M. et al. (2012) in Product Citations). Immunoprecipitation (IP): - Rat sinoatrial cells (SANs) (see Qu, J. et al. (2004) in Product Citations). Immunocytochemistry (IC): - Rabbit carotid body chemoreceptor cells (see Colinas, O. et al. (2008) in Product Citations).|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.6 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
|Formulation||Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
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Provided below are standard protocols that you may find useful for product applications.
KCNE2 (or MiRP1) is a member of a family of proteins that regulate the activity of voltage-dependent K+ channels. The other members of the family are KCNE1 (IsK, MiNK), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE5 (MiRP4). KCNE1 is the founding member of the family and KCNE2 was discovered based on its homology with KCNE1.1,2 The KCNE regulatory subunits are small proteins (14- 20 kD) with a type-1 integral membrane topology. It is believed that both the cytoplasmic C-terminus tail and the transmembrane domain are necessary for the interaction with the a subunits. The stoichiometry of the KCNE subunits with their partner a subunits in the native channels is not clear and ratios ranging from 2 to 14 KCNE subunits per 4 a subunits have been proposed.1, 2 KCNE2 is broadly distributed with prominent expression in brain and heart, but also in other tissues such as skeletal muscle, pancreas and kidney. The best described functional association of KCNE2 is with the voltage-gated K+ channel Kv11.1 (HERG). In the heart, complexes of the two proteins constitute the molecular underlay of the cardiac IKr current and mutations in the KCNE2 subunit are associated with cardiac arrhythmias.1 KCNE2 can form complexes with other channels including the K+ channels Kv7.1 (KCNQ1) and Kv4.3 and the hyperpolarization-activated cation channels HCN1 and HCN2. In the stomach Kv7.1/KCNE2 complexes were found to be crucial for acid secretion as well as for the maintenance of structural integrity, and for parietal cell survival.3
References 1. Abbott, G.W. et al. (1999) Cell 97, 175. 2. Abbott, G.W. and Goldstein, S.A.N. (2001) Mol. Interv. 1, 95. 3. Roepke, T.K. et al. (2006) J. Biol. Chem. 281, 23740.
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