The GLRA1 (glycine receptor α 1) gene is mapped to human chromosome 5q33.1. Glycine receptor is a pentameric Cys-loop ligand-gated ion channel. It is a transmembrane protein, with its five subunits arranged around a central water-filled Cl−selective pore. The protein is expressed all over the nervous system. Each of its subunit contains four transmembrane (TM) segments with an intracellular loop connecting TM3 and TM4, and an extracellular ligand binding domain.
Specificity
The antibody recognizes the α1 glycine receptor and cross-reacts with human α2 glycine receptor subunits.
Immunogen
synthetic peptide from the amino terminus of the human α1 glycine receptor subunit.
Application
Anti-Glycine Receptor antibody is suitable for western blot analysis of immunoprecipitates of rat spinal cord (lane 2) and human sperm extract in the detection of GlyR in human sperm.
Biochem/physiol Actions
Glycine receptors act as excitatory neurotransmitter as well as inhibitory receptor. It plays a central role in acrosome reaction (AR). Mutations in the GLRA1 gene encoding the α1-subunit of the glycine receptor causes startle disease (STHE), also known as hereditary hyperekplexia or congenital stiff-person syndrome.
Physical form
Lyophilized powder from 5 mM ammonium bicarbonate.
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The glycine receptor chloride channel (GlyR) is a member of the nicotinic acetylcholine receptor family of ligand-gated ion channels. Functional receptors of this family comprise five subunits and are important targets for neuroactive drugs. The GlyR is best known for
In this work, we describe a process for production of a Pichia pastoris strain which overproduces large quantities of the human glycine receptor. Subsequent purification yielded functional, uniform protein with expression yields of up to 5 mg per liter cell
Identification of the microdeletion breakpoint in a GLRA1null allele of Turkish hyperekplexia patients.
Becker K, et al.
Human Mutation, 27(10), 1061-1062 (2006)
Disruption of a putative intersubunit electrostatic bond enhances agonist efficacy at the human ?1 glycine receptor.
Welsh B T, et al.
Brain Research, 1657, 148-155 (2017)
Investigating the mechanism by which gain-of-function mutations to the ?1 glycine receptor cause hyperekplexia.
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