GABRA1 Antibody
(Synonyms: Gamma-aminobutyric acid receptor subunit alpha-1, GABA(A) receptor subunit alpha-1, GABAAR subunit alpha-1, GABRA1)GABRA1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to GABRA1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 |
Product Details
GABRA1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to GABRA1.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 55 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 51 kDa
Synthetic peptide corresponding to the center region of human GABRA1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
GABRA1 is an Alpha subunit of the heteropentameric ligand-gated chloride channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain. GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient. Alpha-1/GABRA1-containing GABAARs are largely synaptic (By similarity). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (By similarity). GABAARs containing alpha-1 and beta-2 or -3 subunits exhibit synaptogenic activity; the gamma-2 subunit being necessary but not sufficient to induce rapid synaptic contacts formation. GABAARs function also as histamine receptor where histamine binds at the interface of two neighboring beta subunits and potentiates GABA response (By similarity). GABAARs containing alpha, beta and epsilon subunits also permit spontaneous chloride channel activity while preserving the structural information required for GABA-gated openings (By similarity). Alpha-1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Together with rho subunits, may also control neuronal and glial GABAergic transmission in the cerebellum (By similarity)[1][2][3][4].
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Subcellular Localization
Postsynaptic cell membrane; Cell membrane; Cytoplasmic vesicle membrane
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Isoforms & Post-Translational Modification
GABRA1 has an amino acid length of 456, molecular weight is 51802 Da.
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Subunit
Heteropentamer, formed by a combination of alpha (GABRA1-6), beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho (GABRR1-3), pi (GABRP) and theta (GABRQ) subunits, each subunit exhibiting distinct physiological and pharmacological properties.
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SwissProt ID
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Synonyms
Gamma-aminobutyric acid receptor subunit alpha-1, GABA(A) receptor subunit alpha-1, GABAAR subunit alpha-1, GABRA1
Documentation
[1]. Fuchs C, et al. GABA(A) receptors can initiate the formation of functional inhibitory GABAergic synapses. Eur J Neurosci. 2013 Oct;38(8):3146-58. [Content Brief]
[2]. Brown LE, et al. Inhibitory synapse formation in a co-culture model incorporating GABAergic medium spiny neurons and HEK293 cells stably expressing GABAA receptors. J Vis Exp. 2014 Nov 14;(93):e52115. [Content Brief]
[3]. Zhu S, et al. Structure of a human synaptic GABA(A) receptor. Nature. 2018 Jul;559(7712):67-72. [Content Brief]
[4]. Laverty D, et al. Cryo-EM structure of the human α1β3γ2 GABA(A) receptor in a lipid bilayer. Nature. 2019 Jan;565(7740):516-520. [Content Brief]