|Reactivity||Human, Mouse, Rat|
|Calculated MW||31242 Da|
|Homology||Rat - identical; human - 11/13 amino acid residues identical.|
|Other Names||Voltage-gated hydrogen channel 1, Hydrogen voltage-gated channel 1, HV1, Voltage sensor domain-only protein, mVSOP, Hvcn1, Bts, Vsop|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)GDDYHTWNVNYKK, corresponding to amino acid residues 32-44 of mouse HVCN1 (Accession Q3U2S8). Intracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Application Details||Western blot analysis (WB): - Mouse bone marrow dendritic cell lysate (1:200) (see Szteyn, K. et al. (2012) 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.|
|Buffer After Reconstitution|
|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. Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.|
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Currents measured from voltage-gated proton channels were detected1 long before the channel (HVCN1, also known as Hv1 and VSOP) was cloned2,3. HVCN1 has four membrane spanning domains and intracellular N- and C-termini. Interesting aspects of HVCN1 is that unlike its voltage-gated ion channel counterparts, it has no pore domain4. Also, functional HVCN1 channels are formed by dimers where each monomer has its own conducting pore, each with its own voltage sensor (voltage sensing occurs similarly to other voltage-gated ion channels)5-8. The fundamental role of HVCN1 is to pump out protons, thereby increasing the intracellular pH. The channel is exclusively selective for H+ and opens upon membrane depolarization, although its open state hugely depends on the pH on both sides of the membrane4. Its role is best described in leukocytes where phosphorylation via PKC on a Thr residue potentiates the activity of the channel and increases its open state, thereby increasing the H+ current across the membrane, in this manner mediating optimal NADPH-oxidase (whose optimal activity is at pH 7.5) required for the production of reactive oxygen species (ROS) necessary for phagocytosis to occur4. Apart from leukocytes, HVCN1 is also expressed in basophils where its activation mediates histamine release4,9. In B cells, it maintains optimal signaling, such that ROS production is maintained high10. HVCN1 was found to regulate human spermatozoa activation. Finally, in the airway mucosa, where it regulates pH, channel gating there, is mostly mediated by differences in pH across the membrane as opposed to the membrane potential4.
References 1. DeCoursey, T.E. (1991) Biophys. J. 60, 1243. 2. Ramsey, I.S. et al. (2006) Nature 440, 1213. 3. Sasaki, M. et al. (2006) Science 312, 589. 4. Capasso, M. et al. (2011) Trends Cell Biol. 21, 20. 5. Koch, H.P. et al. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 9111. 6. Lee, S.Y. et al. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 7692. 7. Tombola, F. et al. (2008) Neuron 58, 546. 8. Demaurex, N. and El Chemaly, A. (2010) J. Physiol. 588.23, 4659. 9. Musset, B. et al. (2008) Proc. Natl. Acad. Sci. U.S.A.105, 11020. 10. Schilling, T. et al. (2002) J. Physiol. 545, 93.
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