GALR2 Membrane Protein Introduction

Introduction of GALR2

The GalR2 receptor was first cloned from a rat, it contains 372 amino acid residues and its coding gene has an intron. Exon 1 encodes from the N-terminus of the receptor to the end of the third transmembrane segment, and exon 2 encodes the second intracellular loop to the C-terminus. The extracellular domain of the rat GalR2 receptor has three nitrogen-linked glycosylation sites, while the intracellular domain has a different phosphorylation site than the GalR1 receptor. The C-terminus of the human GalR2 receptor is 15 amino acid residues more than the GalR2 receptor in the rat, and its GalR1 and GalR2 receptors are only about 42% homologous, suggesting that these two receptors have different regulatory functions.

Basic Information of GALR2
Protein Name	Galanin receptor type 2
Gene Name	GALR2
Aliases	GAL2-R, GALNR2, GALR-2, Galanin receptor 2
Organism	Homo sapiens (Human)
UniProt ID	P47211
Transmembrane Times	7
Length (aa)	387
Sequence	MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTT NLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVS LDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWS APRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILI VAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFR KGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQ PCILEPCPGPSWQGPKAGDSILTVDVA

Function of GALR2 Membrane Protein

GalR2 receptors may be coupled to Gq/11 proteins. They activate phospholipase C and promote synaptic transmission efficiency in GalR2 receptor expressing neurons. In addition, GalR2 receptors and forskolin are activated in CHO and HEK293 cells. The cAMP is conjugated and coupled to PKC-dependent MAPK activation in CHO cells, both of which are PTX-sensitive. These characteristics are coupled with Gi-coupled adenylyl cyclase inhibition and Go-coupled MAPK activation, indicating that the GalR2 receptor is also coupled to the Gi/o protein.

Fig.1 Neurons release GAL following injury or inflammation and activate tumour-expressed GALR2. (Scanlon, 2012)

Application of GALR2 Membrane Protein in Literature

Metcalf C.S., et al. Preclinical Analgesic and Safety Evaluation of the GalR2-preferring Analog, NAX 810-2. Neurochem Res. 2017, 42(7): 1983-1994. PubMed ID: 28382595

This article reports that the galanin analog NAX 810-2 has a good preclinical character as a novel and first class analgesic.
Metcalf C.S., et al. Preclinical evaluation of intravenous NAX 810-2, a novel GalR2-preferring analog, for anticonvulsant efficacy and pharmacokinetics. Epilepsia. 2017, 58(2): 239-246. PubMed ID: 28098336

This article reveals that NAX 810-2 effectively activates GalR2 at therapeutic concentrations.
Hui W.Q., et al. Homology modeling, docking, and molecular dynamics simulation of the receptor GALR2 and its interactions with galanin and a positive allosteric modulator. J Mol Model. 2016, 22(4): 90. PubMed ID: 27021209

The article reveals that the mechanism for the allosteric modulation caused by PAMs is the binding of the PAM at pocket III, which is formed by galanin, ECL2, TM2, TM3, and ECL1, which results in the disruption of the Na(⁺)-binding site and/or the Na(⁺) ion pathway, leading to GALR2 agonism.
Metcalf C.S., et al. Analgesic properties of a peripherally acting and GalR2 receptor-preferring galanin analog in inflammatory, neuropathic, and acute pain models. J Pharmacol Exp Ther. 2015, 352(1): 185-93. PubMed ID: 25347995

This article shows that nonbrain-penetrating galanin analog reduces pain behaviors in several models and does not produce some of the dose-limiting toxicities associated with other analgesics.
Banerjee R., et al. The G protein-coupled receptor GALR2 promotes angiogenesis in head and neck cancer. Mol Cancer Ther. 2014, 13(5): 1323-33. PubMed ID: 24568968

This article evaluates that GALR2 stimulates tumor angiogenesis in SCCHN via p38-mediated inhibition of TTP with resultant enhanced cytokine secretion.

GALR2 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-GALR2 antibody development services.

As a forward-looking research institute as well as a leading customer service provider in the field of membrane protein, Creative Biolabs has won good reputation among our worldwide customers for successfully accomplishing numerous challenging projects including generation of many functional membrane proteins. Please feel free to contact us for more information.

Reference

Scanlon CS, et al. (2012). Galanin modulates the neural niche to favour perineural invasion in head and neck cancer. Nature Communications. 28(6), 6885.

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