Our Anti-Gephyrin mouse monoclonal primary antibody from NeuroMab is produced in-house from hybridoma clone L106/83. It detects human, mouse, and rat Gephyrin, and is purified by Protein A chromatography. It is great for use in AT, IHC, ICC, WB.
Array tomography immunofluorescence of an LRWhite-embedded 70 nm section from adult mouse cortex with L106/83 (green), rabbit mAb GAD2 (Cell Signaling #5843, magenta) and DAPI (blue). The insert shows three consecutive sections through the synapse that is marked with a white box. Image courtesy of Kristina Micheva (Stanford).
In neuronal tissue, gephyrin is a scaffolding protein that self assembles in a complex, flat submembraneous lattice that inhibits mobility of the glycine receptors (GlyR) and GABAA receptors (GABAAR) causing clustering at post synaptic sites (Groeneweg et al, 2018). In non-neuronal tissue gephyrin plays a critical role in the molybdendum cofactor (MoCo) biosynthesis of essential life molybdoenzymes, like sulphite oxidase (Groeneweg et al, 2018). Three functional domains have been identified in gephyrin: the stable, structural G and E domains, and the C domain which is intrinsically unstructured leading to multiple isoforms (108, 105, 102, 98, 90 kDa) (Kawasaki, et al 1997). The 93 kDa protein predominantly expressed in the brain and located in the plasma membrane, has a 10X stronger affinity for the GlyR than the GABAAR. Gephyrin’s flexibility to change its size and molecular density is directly correlated to its high affinity to the GlyR-β subunit, and is required for anchoring and accurate clustering of GlyRs at post synaptic sites and microtubule transport chains (Greoneweg et al, 2018). A consistent parameter in the pathogenesis of Alzheimers Disease shows a decrease of inhibitory GABAergic synapses and gephyrin, and increased levels of an insoluble 37 kDa gephyrin fragment not detected in healthy, non-AD models (Kiss et al, 2016).
Purified by Protein A chromatography
1 mg/mL
Monoclonal
L106/83
IgG2b
ICC, IHC, WB
Mouse
GPHN GPH KIAA1385
80 kDa
Fusion protein amino acids 1-181 (N-terminus) of human Gephyrin (accession number Q9NQX3) produced recombinantly in E. Coli
Human, Mouse, Rat
AB_2636851
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.125
WB: 1:1000
IHC: 1:100
Unconjugated
No cross-reactivity reported
Each new lot of antibody is quality control tested by western blot on rat whole brain lysate and confirmed to stain the expected molecular weight band.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
Micheva, K.D., et al. 2021. Conduction velocity along the local axons of parvalbumin interneurons correlates with the degree of axonal myelination. Cerebral Cortex, 3374-3392.
Simhal, A.K., et al. 2019. Multifaceted changes in synaptic composition and astrocytic involvement in a mouse model of fragile X syndrome. Scientific Reports, 13855.
Gruol, DL, et al. 2023. Impact of Elevated Brain IL-6 in Transgenic Mice on the Behavioral and Neurochemical Consequences of Chronic Alcohol Exposure. Cells, 0.
Gruol, D.L., et al. 2020. Alcohol and IL-6 Alter Expression of Synaptic Proteins in Cerebellum of Transgenic Mice With Increased Astrocyte Expression of IL-6. Neuroscience, 124-137.
Gruol, D.L., et al. 2018. Altered Brain Activity During Withdrawal from Chronic Alcohol is Associated with Changes in IL-6 Signal Transduction and GABAergic Mechanisms in Transgenic Mice with Increased Astrocyte Expression of IL-6. Neuropharmacology., 32-46.
Gruol, D.L., et al. 2018. Altered brain activity during withdrawal from chronic alcohol is associated with changes in IL-6 signal transduction and GABAergic mechanisms in transgenic mice with increased astrocyte expression of IL-6. Neuropharmacology, 32-46.
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