Grik1 Antibody is affinity chromatography purified via peptide column.
Immunogen
Grik1 antibody was raised against a 16 amino acid synthetic peptide near the center of the human Grik1. The immunogen is located within amino acids 380 - 430 of Grik1.
Grik1 antibody can be used for detection of Grik1 by Western blot at 0.5 - 1 μ,g/mL. Antibody can also be used for immunohistochemistry starting at 2.5 μ,g/mL. For immunofluorescence start at 20 μ,g/mL.
Antibody validated: Western Blot in rat samples, Immunohistochemistry in human samples and Immunofluorescence in human samples. All other applications and species not yet tested.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1 mg/mL
Buffer
Grik1 Antibody is supplied in PBS containing 0.02 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
-20 °C,4 °C
Informationen zur Lagerung
Grik1 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Grik1 Antibody: Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. Grik1, also known as glutamate receptor 5, belongs to the kainate family of glutamate receptors, which are composed of four subunits and function as ligand-activated ion channels. Grik1 is expressed in GABAergic interneurons of the hippocampus and are thought to participate in the formation of various subtypes of kainate receptors with Grik2 and KA2. Stimulation of Grik1 leads to intracellular calcium release and activation of protein kinase C. Excessive activation has been associated with psychiatric, neurological and neurodegenerative diseases. Numerous isoforms of Grik1 are known to exist and may be subject to RNA editing within the second transmembrane domain, which is thought to alter the properties of ion flow.