Recombinant human GPCR GPR35 protein (His tag)
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Recombinant human GPCR GPR35 protein (His tag) is a Human Full Length protein, in the 1 to 309 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
G-protein coupled receptor 35, Kynurenic acid receptor, KYNA receptor, GPR35
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human GPCR GPR35 protein (His tag) (AB314525)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GPR62 participates in cellular signaling by interacting with G proteins to transmit signals inside the cell. Although not well-characterized compared to other GPCRs evidence suggests GPR62 may play a role in modulating neurotransmitter release and brain activity. It does not belong to a known receptor complex but its actions presumably influence neurological pathways related to cognition and mood regulation.
Pathways
Studies indicate GPR62 engages primarily with signaling cascades involved in neuronal communication and response. While its exact pathways are not fully documented links suggest it could affect pathways like the cAMP signaling pathway. GPR62 shares relationships with various neurotransmitter systems and could exhibit interactions with GPR35 and other neuroreceptor partners in these pathways influencing cognitive processes.
Specifications
Form
Lyophilized
General info
Function
G-protein coupled receptor that binds to several ligands including the tryptophan metabolite kynurenic acid (KYNA), lysophosphatidic acid (LPA) or 5-hydroxyindoleacetic acid (5-HIAA) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways (PubMed : 16754668, PubMed : 19473985, PubMed : 20361937, PubMed : 24347166, PubMed : 35148838, PubMed : 35926043). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed : 19473985, PubMed : 35926043). GPR35 can couple with G(i)/G(o)- or G(12)/G(13) classes of G alpha proteins depending on the context, mediating the inhibition of adenylate cyclase or activation Rho small GTPases, respectively (PubMed : 19473985, PubMed : 35926043, PubMed : 36543774). KYNA-binding promotes monocyte adhesion to vascular endothelium under flow conditions, leading to G(i)/GNAI1 activation and inhibition of adenylate cyclase (PubMed : 19473985). Involved in cardioprotection during ischemia by promoting mitochondrial remodeling : following KYNA-binding and G(i)/GNAI1 activation, GPR35 is internalized to the outer mitochondrial membrane, where it inhibits mitochondrial adenylate cyclase (ADCY10), allowing ATPIF1 to repress ATP synthase activity (PubMed : 35926043). Stimulates lipid metabolism, thermogenic and anti-inflammatory gene expression in adipose tissue once activated by KYNA (By similarity). Plays a role in neutrophil recruitment to sites of inflammation and bacterial clearance through the major serotonin metabolite 5-HIAA that acts as a physiological ligand (PubMed : 35148838). In macrophages, activation by lysophosphatidic acid promotes GPR35-induced signaling with a distinct transcriptional profile characterized by TNF production associated with ERK and NF-kappa-B activation (By similarity). In turn, induces chemotaxis of macrophages (By similarity).
Sequence similarities
Belongs to the G-protein coupled receptor 1 family.
Post-translational modifications
Multiply phosphorylated in clusters of serines and threonines in the C-terminal tail (PubMed:35101446). Phosphorylation of Ser-300 and Ser-303 is mediated by GRK5 and/or GRK6 (PubMed:37660910).
Target data
Product promise
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