|Application ||WB, IHC, IP, ICC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||48652 Da|
|Homology||Rat - 40/41 amino acid residues identical; golden hamster - 39/41 amino acid residues identical; human - 37/41 amino acid residues identical.|
|Other Names||G protein-activated inward rectifier potassium channel 2, GIRK-2, Inward rectifier K(+) channel Kir32, Potassium channel, inwardly rectifying subfamily J member 6, Kcnj6, Girk2, Kcnj7, W|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||GST fusion protein with sequence ELANRAEVPLSWSVS SKLNQHAELETEEEEKNPEELTERNG, corresponding to residues 374-414 of mouse Kir3.2 (Accession P48542), (MW: 31 kDa.). Intracellular, C-terminal part.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl PBS.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||3 µg fusion protein per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Kir3.2 (or G-protein regulated Inward-Rectifier K+ channel, GIRK2) is a member of the family of inward rectifying K+ channels. The family includes 15 members that are structurally and functionally different from the voltage-dependent K+ channels. The family’s topology consists of two transmembrane domains that flank a single and highly conserved pore region with intracellular N- and C-termini. As is the case for the voltage-dependent K+ channels the functional unit for the Kir channels is composed of four subunit that can assembly as either homo or heterotetramers. Kir channels are characterized by a K+ efflux that is limited by depolarizing membrane potentials thus making them essential for controlling resting membrane potential and K+ homeostasis. Kir3.2 is a member of the Kir3.x subfamily that includes four members (Kir3.1- Kir3.4). The Kir3 family is characterized by the fact that the channels can be activated by neurotransmitters and other factors acting via the activation of G-protein coupled receptors. Binding of the corresponding ligand to the G-protein receptor induces the dissociation of Gα-GTP from the Gbg dimer. The latter directly binds to Kir3 and activates the channel.2,3 Kir3.2 is mainly expressed in the brain, were it co-assembles with Kir3.1 or Kir3.3 and mediates the inhibitory effects of many neurotransmitters including opioid, adrenergic, muscarinic, dopaminergic and γ-aminobutyric acid (GABA).2,3 Point mutations in the mouse Kir3.2 channel cause the weaver (wv) phenotype, a neurological abnormality characterized by the abnormal ‘weaving’ of the mice when they walk, hence the name weaver which is due to a substantial loss of cerebellar granule neurons. These mice also display mild local motor hyperactivity, presumably caused by the degeneration of dopaminergic neurons in the substantia nigra, spontaneous seizures and male sterility.1 A peptide toxin originating from the Apis mellifera bee venom, Tertiapin (#STT-250) was shown to be a potent blocker of Kir3.2 containing channels (7 nM for Kir3.2 alone and 5.4 nM for the Kir3.1/3.2 combination).4
1. Hess, E.J. (1996) Neuron 16, 1073.
2. Dascal, N. (1997) Cell Signal. 9, 551.
3. Mark, M.D. et al. (2000) Eur. J. Biochem. 267, 5830.
4. Kubo, Y. et al. (2005) Pharmacol. Rev. 57, 509.
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