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GLRB encodes the beta subunit of the glycine receptor, which is a pentamer composed of alpha and beta subunits. Additionally we are shipping GLRB Proteins (6) and many more products for this protein.
Showing 10 out of 40 products:
Human Polyclonal GLRB Primary Antibody for EIA, WB - ABIN952548
Ziegler, Bodusch, Song, Jahn, Wolfes, Steinlechner, Dengler, Bufler, Krampfl: Interaction of androsterone and progesterone with inhibitory ligand-gated ion channels: a patch clamp study. in Naunyn-Schmiedeberg's archives of pharmacology 2009
Show all 2 references for 952548
Human Polyclonal GLRB Primary Antibody for ELISA, WB - ABIN1451271
Milani, Mülhardt, Weber, Lichter, Kioschis, Poustka, Becker: The human glycine receptor beta subunit gene (GLRB): structure, refined chromosomal localization, and population polymorphism. in Genomics 1998
Rat (Rattus) Monoclonal GLRB Primary Antibody for ICC, IHC - ABIN1742318
Weltzien, Puller, OSullivan, Paarmann, Betz: Distribution of the glycine receptor β-subunit in the mouse CNS as revealed by a novel monoclonal antibody. in The Journal of comparative neurology 2012
Whole-exome sequencing in ASD (show ARSD Antibodies) patients from each family identified a second rare inherited genetic variant, affecting GLRB expressed in inhibitory or in excitatory synapses.
GLRA1 (show GLRA1 Antibodies) and GLRB mutations are responsible for abnormal startled reactions in humans. (Review)
The N-terminal region of GABRA3 (show GABRA3 Antibodies) and the GlyR beta subunit (show POLG Antibodies) occupies the same binding site of gephyrin (show GPHN Antibodies).
We report novel GLRB mutations in hyperekplexia
Systematic DNA sequencing of GLRB in individuals with hyperekplexia revealed new missense mutations in GLRB, resulting in M177R, L285R and W310C substitutions.
This study describes the definitive assignment of GLRB as the third major gene for hyperekplexia and impacts on the genetic stratification and biological causation of this neonatal/paediatric disorder.
investigated neural progenitor cells in respect to their glycine receptor function and subunit expression using electrophysiology, calcium imaging, immunocytochemistry, and quantitative real-time PCR
Distinct properties of glycine receptor beta+/alpha- interface: unambiguously characterizing heteromeric interface reconstituted in homomeric protein.
This study presents a large family with Hereditary hyperekplexia (HH) as a result of homozygous mutation in GLRB.
Hereditary hyperekplexia-causing mutations that modify alpha1 beta GlyR channel function are almost exclusively located in the alpha1 to the exclusion of the beta subunit (show POLG Antibodies).
A species-specific thymine-to-guanine sequence variation in the Glrb gene has been identified which gives rise to species-specific splice donor sites in the Glrb genes of mouse and bushbaby.
The SdpI (show PACSIN1 Antibodies)-binding site was mapped to a proline-rich sequence of 22 amino acids within the intracellular loop of GlyRbeta.
These results show that insulin (show INS Antibodies) has a novel regulatory action on the potency of glycine for ionotropic glycine receptors.
Visual stimulation regulates maturation of retinal ganglion cell synaptic activity and connectivity primarily through glycine receptor-mediated synaptic transmission.
This gene encodes the beta subunit of the glycine receptor, which is a pentamer composed of alpha and beta subunits. The receptor functions as a neurotransmitter-gated ion channel, which produces hyperpolarization via increased chloride conductance due to the binding of glycine to the receptor. Mutations in this gene cause startle disease, also known as hereditary hyperekplexia or congenital stiff-person syndrome, a disease characterized by muscular rigidity. Alternative splicing results in multiple transcript variants.
glycine receptor, beta
, glycine receptor subunit beta
, glycine receptor subunit beta-like
, glycine receptor 58 kDa subunit
, glycine receptor, beta subunit
, glycine receptor beta
, inhibitory glycine receptor