GABBR1 Antibody
(Synonyms: GPRC3A, GABBR1, Gamma-aminobutyric acid type B receptor subunit 1, GABA-B receptor 1, GABA-B-R1, GABA-BR1, GABABR1, Gb1)GABBR1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to GABBR1.
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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
GABBR1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to GABBR1.
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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: 110; 130 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: 108 kDa
Synthetic peptide corresponding to the C-term region of human GABBR1.
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
GABBR1 is a Component of a heterodimeric G protein-coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen[1][2][3][4][5][6][7][8][9][10][11].
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Subcellular Localization
Cell membrane; Postsynaptic cell membrane; Cell projection, dendrite
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Expression
Tissue_Specificity: Highly expressed in brain. Weakly expressed in heart, small intestine and uterus. Isoform 1A: Mainly expressed in granular cell and molecular layer. Isoform 1B: Mainly expressed in Purkinje cells. Isoform 1E: Predominantly expressed in peripheral tissues as kidney, lung, trachea, colon, small intestine, stomach, bone marrow, thymus and mammary gland. -
Isoforms & Post-Translational Modification
GABBR1 has 5 isoforms, Q9UBS5-1: amino acid length is 961, molecular weight is 108320 Da (predicted); Q9UBS5-2: amino acid length is 844, molecular weight is 95148 Da (predicted); Q9UBS5-3: amino acid length is 899, molecular weight is 101543 Da (predicted); Q9UBS5-4: amino acid length is 931, molecular weight is 104665 Da (predicted); Q9UBS5-5: amino acid length is 578, molecular weight is 65082 Da (predicted).
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Subunit
Heterodimer of GABBR1 and GABBR2.
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SwissProt ID
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Synonyms
GPRC3A, GABBR1, Gamma-aminobutyric acid type B receptor subunit 1, GABA-B receptor 1, GABA-B-R1, GABA-BR1, GABABR1, Gb1
Documentation
[1]. Villemure JF, et al. Subcellular distribution of GABA(B) receptor homo- and hetero-dimers. Biochem J. 2005 May 15;388(Pt 1):47-55. [Content Brief]
[2]. Nomura R, et al. Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor. J Biol Chem. 2008 Feb 22;283(8):4665-73. [Content Brief]
[3]. Geng Y, et al. Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2. Nat Neurosci. 2012 Jun 3;15(7):970-8. [Content Brief]
[4]. Geng Y, et al. Structural mechanism of ligand activation in human GABA(B) receptor. Nature. 2013 Dec 12;504(7479):254-9. [Content Brief]
[5]. Cediel ML, et al. GABBR1 monoallelic de novo variants linked to neurodevelopmental delay and epilepsy. Am J Hum Genet. 2022 Oct 6;109(10):1885-1893. [Content Brief]
[6]. White JH, et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature. 1998 Dec 17;396(6712):679-82. [Content Brief]
[7]. Kuner R, et al. Role of heteromer formation in GABAB receptor function. Science. 1999 Jan 1;283(5398):74-7. [Content Brief]
[8]. Ng GY, et al. Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity. J Biol Chem. 1999 Mar 19;274(12):7607-10. [Content Brief]
[9]. Sullivan R, et al. Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B)) receptors with truncated receptors and metabotropic glutamate receptor 4 supports the GABA(B) heterodimer as the functional receptor. J Pharmacol Exp Ther. 2000 May;293(2):460-7. [Content Brief]
[10]. Schwarz DA, et al. Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1) splice variant encoding a truncated receptor. J Biol Chem. 2000 Oct 13;275(41):32174-81. [Content Brief]
[11]. Kaupmann K, et al. Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels. Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):14991-6. [Content Brief]