This antibody is predicted to have no cross-reactivity to ORAI1 or ORAI2.
Aufreinigung
ORAI3 Antibody is affinity chromatography purified via peptide column.
Immunogen
ORAI3 antibody was raised against a 15 amino acid synthetic peptide from near the amino terminus of human ORAI3. The immunogen is located within the first 50 amino acids of ORAI3.
ORAI3 antibody can be used for detection of ORAI3 by Western blot at 1 - 4 μ,g/mL. Antibody can also be used for immunocytochemistry starting at 10 μ,g/mL and Immunohistochemistry starting at 2 μ,g/mL
Antibody validated: Western Blot in mouse samples, Immunohistochemistry in mouse samples and Immunocytochemistry in mouse samples. All other applications and species not yet tested.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1 mg/mL
Buffer
ORAI3 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
ORAI3 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.
ORAI3 Antibody: Antigen stimulation of immune cells triggers Ca++ entry through Ca++ release-activated Ca++ (CRAC) channels. ORAI3 is one of two mammalian homologs to ORAI1, a recently identified four-transmembrane spanning protein that is an essential component of CRAC. All three homologs have been shown to function as Ca++ plasma membrane channels gated through interactions with STIM1, the store-activated endoplasmic reticulum Ca++ sensor. However, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter.