Recombinant Human ASIC1 protein is a Human Fragment protein, in the 83 to 301 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear. Isoform 1 does not display proton-gated cation channel activity.
ACCN2, BNAC2, ASIC1, Acid-sensing ion channel 1, Brain sodium channel 2, BNaC2
Recombinant Human ASIC1 protein is a Human Fragment protein, in the 83 to 301 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Constituents: 0.58% Sodium chloride, 0.32% Tris HCl
Purified via His tag
Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear.
Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC1 subfamily.
Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel.
The ASIC1 or acid-sensing ion channel 1 is also known as ASIC or ACCN2. It is part of a group of proton-gated cation channels. ASIC1 has a molecular mass of approximately 60 kDa. This ion channel plays a role in the detection of acidosis where it mediates proton influx across cell membranes affecting changes in membrane potential. ASIC1 is expressed in neurons of the central and peripheral nervous systems with particular abundance in the brain. Its localization to regions such as the amygdala suggests a possible role in processing emotions and pain perception.
This ion channel aids in neuronal response to pH drops serving as a sensor for acidification. The ASIC1 subunit can form homotrimers or heterotrimers with other ASIC subunits which impacts the ion conductance properties. This protein's activity affects synaptic plasticity and is involved in both short-term and long-term modulation of neuronal circuits. Changes in its activity can influence neurotransmission and has implications in neurological functionality.
ASIC1 is part of the neurophysiological signaling pathways affecting synaptic transmission. It interacts with other proteins like ASIC2 and ASIC3 being implicated in the modulation of sensory perception and pain. Involvement in pathways like the pain-transducing signaling pathway places ASIC1 in a context where it can regulate nociceptive signals. It participates in ion flux alterations that contribute to neuronal excitability and synaptic strength.
ASIC1 has connections to neurodegenerative conditions and pain syndromes. It is implicated in the pathophysiology of disorders such as ischemia where acidosis occurs during stress and tissue damage and chronic pain conditions. ASIC1 interacts with proteins such as the NMDA receptor in the context of these diseases suggesting a role in excitotoxicity. Dysfunction or altered regulation of ASIC1 may exacerbate neurodegeneration or chronic pain symptoms highlighting its potential as a therapeutic target.
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