Specific for the ~48 kDa alpha 1 and alpha 2 subunits of the Glycine Receptor in Western blots of rat spinal cord, brain stem and cell extracts. Immunolabeling is blocked by preadsorption of antibody with the peptide immunogen. This antibody does not recognize other Glycine Receptor subunits.
Polyclonal Rabbit IgG
Peptide from the N-terminus region of the alpha 1 subunit of the rat Glycine Receptor
Lyophilized in 5 mM ammonium bicarbonate
Frozen sections; unpublished observations, 1:1000
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Rat Glycine R by Western Blot. Western blot of 10 μg of rat spinal cord. As shown in the autoradiograph, the Anti-Glycine Receptor antibody is specific for the ~48 kDa subunits recognizing both the alpha 1 and alpha 2 subunits of the Glycine Receptor.
Preparation and Storage
This antibody should be reconstituted in 100 μL phosphate buffered saline (137 mM NaCl, 7.5 mM Na2HPO4, 2.7 mM KCl, 1.5 mM KH2PO4, pH 7.4) before use.
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
The lyophilized product is stable at ≤- 20° C for at least 1 year. After reconstitution the antibody should be aliquoted and stored at ≤ -20° C.
Background: Glycine R
The rat glycine receptor (GlyR) chloride channel is a member of the nicotinic acetylcho-line receptor family of ligand-gated ion channels. Its glycine-mediated activation results in an influx of chlorine ions that hyperpolarize and desensitize neuronal postsynaptic membranes. The receptor’s multimeric makeup is unclear. It may be either a three or five subunit homo- or heteromultimer. To date, there are five rat GlyR subunit types. Four are 48-53 kDa alpha -type subunits, and one is a 58 kDa beta -type subunit. Alternate splicing exists for alpha 1 and alpha 2 subunit types. Alpha-type subunits may form homotrimers; however, their function may not be neurotransmission but rather non-synaptic cell-cell communication. Alpha1-beta multimers may be the principal synaptic GlyR in adults.