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HVCN1 encodes a voltage-gated protein channel protein expressed more highly in certain cells of the immune system. Additionally we are shipping HVCN1 Antibodies (41) and HVCN1 Proteins (3) and many more products for this protein.
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Our data demonstrated that the expression of Hv1 in pancreatic islet beta-cells regulates insulin (show INS ELISA Kits) secretion through regulating Ca(2 (show CA2 ELISA Kits)+) homeostasis.
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]
Hv1 activity displays hysteresis
A shorter isoform of HVCN1 with enhanced gating is specifically enriched in malignant B cells.
Divalent metal binding causes a conformational change in human the Hv1 c-terminal domain.
analysis of of the C-terminal domain of voltage-gated proton channel HV1 and the thermodynamic characteristics of Zn(2) binding to this domain
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.
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.
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 activity
In the Hv1 voltage-gated channel a highly conserved phenylalanine is found in the charge transfer center.
Alkalinity of neutrophil phagocytic vacuoles is modulated by HVCN1.
The voltage-gated proton channel Hv1/VSOP inhibits neutrophil granule release
Eosinophils require proton channel HVCN1 for optimal reactive oxygen species generation and prevention of activation-induced cell death.
Functional expression of voltage-gated proton (Hv1) channels is characterized, for the first time, in mouse bone marrow-derived dendritic cells.
inhibition of Hv1 function via knockdown of Hv1 expression can effectively retard cancer growth
Hv1 channels maintain a physiological membrane potential during the respiratory burst of neutrophils by providing a compensating charge for the electrons transferred by NOX2 (show CYBB ELISA Kits) from NADPH (show FDXR ELISA Kits) to superoxide.
Review of structural organization and gating of Hv1 channels discusses relationship between gating of Hvcn1 and the gating of ion-conducting pores recently discovered in the voltage-sensing domains of mutant voltage-gated potassium and sodium channels.
HVCN1 -deficieent B cells show a defct in ROS production, which causes less signal transduction through impaired BCR-dependent oxidation of SHP-1.
Hv1 channels truncated just downstream of R2 in the S4 segment retain most channel properties.
This gene encodes a voltage-gated protein channel protein expressed more highly in certain cells of the immune system. Phagocytic cells produce superoxide anions which require this channel protein, and in B cells this same process facilitates antibody production. This same channel protein, however, can also regulate functions in other cells including spermatozoa. Multiple transcript variants encoding different isoforms have been found for this gene.
, voltage-gated hydrogen channel 1
, hydrogen voltage-gated channel 1
, voltage sensor domain-only protein