HVCN1; VSOP; UNQ578/PRO1140; Voltage-gated hydrogen channel 1; Hydrogen voltage-gated channel 1; HV1; Voltage sensor domain-only protein
Species
Homo sapiens (Human)
Source
in vitro E.coli expression system
Expression Region
1-273
Target Protein Sequence
MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPT PVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAEL ILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVV SFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAA KIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis.
Gene References into Functions
The authors now report that R1H mutation is sufficient to reconstitute resting-state H(+) 'shuttle' conductance in Hv1 without abrogating the intrinsic 'aqueous' H(+) conductance.PMID:27572256
We suggest that cleavage and heterodimerization of Hv1 represents an adaptation to the specific requirements of pH control in sperm.PMID:27859356
CREBBP mutations were associated with inferior progression-free survival (PFS), whereas mutations in previously unreported HVCN1, a voltage-gated proton channel-encoding gene and B-cell receptor signaling modulator, were associated with improved PFS.PMID:28064239
Trp207 is crucial for slow channel opening, highly temperature-dependent gating kinetics, proton selectivity, and DeltapH-dependent gating.PMID:26458876
Our data demonstrated that the expression of Hv1 in pancreatic islet beta-cells regulates insulin secretion through regulating Ca(2+) homeostasis.PMID:26559003
The main properties of the voltage-gated proton channel (HV1) are described in this review, along with what is known about how the channel protein structure accomplishes its functions. [review]PMID:25964989
A shorter isoform of HVCN1 with enhanced gating is specifically enriched in malignant B cells.PMID:25425665
Divalent metal binding causes a conformational change in human the Hv1 c-terminal domain.PMID:24867409
analysis of of the C-terminal domain of voltage-gated proton channel HV1 and the thermodynamic characteristics of Zn(2) binding to this domainPMID:25446125
Salt bridge networks and the hydrophobic plug function as the gate in Hv1 channels; outward movement of the fourth transmembrane segment leads to the opening of this gate.PMID:24379371
Results suggest that Hv1 may be used as a potential biomarker for diagnosis and prognosis of colorectal carcinoma, and a potential target for anticancer drugs in colorectal cancer therapy.PMID:23940591
inhibition of Hv1 activity via Zn(2+) ions can effectively retard the cancer growth and suppress the cancer metastasis by the decrease of proton extrusion and the down-regulation of gelatinase activityPMID:23891691
In the Hv1 voltage-gated channel a highly conserved phenylalanine is found in the charge transfer center.PMID:23352164
Two conformational changes are detected in Hv1 channels that are involved in channel opening.PMID:23352165
inhibition of Hv1 function via knockdown of Hv1 expression can effectively retard cancer growthPMID:22367212
Hv1 channels maintain a physiological membrane potential during the respiratory burst of neutrophils by providing a compensating charge for the electrons transferred by NOX2 from NADPH to superoxide.PMID:22056415
Hv1-dependent reactive oxygen species production is responsible for a substantial fraction of brain damage at early time points after ischemic stroke.PMID:22388960
Interactions with two of the S4 arginines and the formation of a well defined hydrophobic gap in the center of the Hv1 are key to the formation of a robust water wire.PMID:21843503
identification of aspartate 112 as a crucial component of the selectivity filter of H(V)1PMID:22020278
these results strongly suggest that Hv1 regulates breast cancer intracellular pH and exacerbates the migratory ability of metastatic cells.PMID:21821008
Data demonstrated that a massive reduction in H(v)1 expression can limit the Nox2 mediated superoxide production of PLB-985 granulocytes.PMID:21124855
The HVCN1 H(+) channel mediates pH-regulated acid secretion by the airway epithelium. Apical HVCN1 represents a mechanism to acidify an alkaline airway surface liquid.PMID:20548053
Report on the interaction of HV1 proton channel protomers during ion channel gating.PMID:20676047
HVCN1 not only modulates signaling from the B-cell receptor following B-cell activation and histamine release from basophils, but also mediates pH-dependent activation of spermatozoa, as well as acid secretion by tracheal epithelium. [Review]PMID:20961760
Molecular dynamics simulations revealed water molecules in the central crevice of Hv1 model structures but not in homologous voltage-sensor domain (VSD) structures.PMID:20543828
In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264).PMID:20147290
Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytesPMID:20037153
Since Hv1 specifically mediates proton efflux, it is likely to be the long-sought molecule that controls male fertility by mediating intracellular alkalinization of human spermPMID:20144758
Hv1 channels truncated just downstream of R2 in the S4 segment retain most channel properties.PMID:20018719
data presented here identify H(v)1 as a long-sought voltage-gated H+ channel and establish H(v)1 as the founding member of a family of mammalian VSD proteinsPMID:16554753
We cloned a new B cell-specific tetraspanning (BTS) membrane moleculePMID:17948262
Hv1 forms a dimer in the membrane;its regions that are close to the dimer interface were defined.PMID:18509058
The Hv1 channel voltage sensor domain by itself supports H(+) flux.PMID:19233200
The C-terminal domain of the human voltage-gated proton channel Hv1 (C-Hv1) was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method.PMID:19255483
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Subcellular Location
Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.
Protein Families
Hydrogen channel family
Tissue Specificity
Enriched in immune tissues, such as lymph nodes, B-lymphocytes, monocytes and spleen.