Cell Line (CPBU)

This is a cell model with luciferase reporter gene for cell-based assay. CHO-K1/CRE-CBLuc/GLP1R Stable cell line is designed for In Vitro assay to detect the bioactivity of GLP-1 analogue. The binding affininity or the relative potency of the candidate drug can also be evaluated with this cell model.

The CRF1 receptor is a Gs-coupled GPCR expressed in the brain and pituitary gland that binds to several neuropeptides, including corticotropin-releasing factor (CRF) and urocortin, and the amphibian peptide sauvagine. CRF plays a predominant role in stress response mediated by the hypothalamic-pituitary-adrenal axis, and alterations in CRF and its receptors CRF1 and CRF2 appear to be linked to depression and anxiety. In comparison to the CRF2 receptor, the CRF1 receptor has received considerable attention as a potential therapeutic target for the treatment of stress-related disorders such as adrenocorticotropin hypersecretion, increased colonic motility and exaggerated fear and anxiety-related behavior.

The corticotropin-releasing factor receptor 2 CRF2 is Gs-coupled GPCRs expressed in the brain, blood vessels and intestine that bind to corticotropin-releasing factor (CRF). The CRF is a 41-amino acid peptide that plays an important role in the integration of autonomic, neuroendocrine, and behavioral responses to stress. GenScript’s cloned human CRF2-expressing cell line co-expressing Gα15 is made in the CHO-K1 host.

Numerous studies have demonstrated that the calcitonin receptor (CALCR) is a specific marker of osteoclast differentiation and that calcitonin can inhibit bone resorption in vitro and in vivo. Mice lacking calcitonin and calcitonin gene-related peptide (CGRP) have a high bone mass phenotype due to an increase in bone formation parameters. Expression of calcitonin (CT) and its receptor (CTR) generate survival, adhesion, pro-inflammatory, and pro-metastatic pathways. Moreover, data indicate a pivotal role for CT-CTR axis in advanced prostate cancer PC metastasis and may serve as a potential therapeutic target for advanced PC.

CTLA4 or CTLA-4 (cytotoxic T-lymphocyte-associated protein 4), also known as CD152 (cluster of differentiation 152), is a protein receptor that functions as an immune checkpoint and downregulates immune responses. CTLA4 is constitutively expressed in regulatory T cells but only upregulated in conventional T cells after activation – a phenomenon which is particularly notable in cancers. It acts as an “off” switch when bound to CD80 or CD86 on the surface of antigen-presenting cells.

The CTLA-4 protein is encoded by the Ctla4 gene in mice and the CTLA4 gene in humans.

CXCR4 is a receptor for the C-X-C chemokine SDF-1 (Stromal Cell-Derived Factor 1). It is involved in haematopoiesis and cardiac ventricular septum formation, and plays an essential role in vascularization of the gastrointestinal tract, cerebellar development and survival of hippocampal-neuron of central nerve system. CXCR4 also acts as a primary receptor for some HIV-2 isolates and as a co-receptor with CD4 for HIV-1 X4 viruses.

4-1BB is a member of the tumor necrosis factor (TNF) receptor family. Its alternative names are tumor necrosis factor receptor superfamily member 9 (TNFRSF9), CD137 and induced by lymphocyte activation (ILA). It is currently of interest to immunologists as a co-stimulatory immune checkpoint molecule. 4-1BB can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, 4-1BB expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation.

BDCA-2 is a novel type II C-type lectin, which shows 50.7% sequence identity at the amino acid level to its putative murine ortholog, the murine dendritic cell–associated C-type lectin 2. In addition to its antigen capturing function, BDCA-2 can mediate potent inhibition of induction of IFN-α/β expression in PDCs. Production of IFN-α/β in response to several different types of viruses, bacteria, CpG-DNA, dsRNA, and SLE serum is by far the most prominent feature of PDCs.

BDCA-2 is a novel type II C-type lectin, which shows 50.7% sequence identity at the amino acid level to its putative murine ortholog, the murine dendritic cell–associated C-type lectin 2. In addition to its antigen capturing function, BDCA-2 can mediate potent inhibition of induction of IFN-α/β expression in PDCs. Production of IFN-α/β in response to several different types of viruses, bacteria, CpG-DNA, dsRNA, and SLE serum is by far the most prominent feature of PDCs.

CD155, commonly known as PVR (poliovirus receptor) and Necl-5 (nectin-like molecule-5), is a type I transmembrane single-span glycoprotein and belongs to the nectins and nectin-like (Necl) subfamily. CD155 was originally identified based on its ability to mediate the cell attachment and entry of poliovirus (PV), an etiologic agent of the central nervous system disease poliomyelitis. The normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. CD155 may assist in an efficient humoral immune response generated within the intestinal immune system. It’s been shown that CD155 can be recognized and bind by DNAM-1 and CD96, which promotes the adhension, migration, and NK-cell killing. Thus, inducing cell-mediated tumor-specific immunity.

This gene encodes a membrane protein, which is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The encoded protein is also a receptor for the C-terminal cell binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This gene has broad tissue, distribution, and is reduced in expression on Rh erythrocytes. Alternatively spliced transcript variants have been found for this gene.

CTLA4 or CTLA-4 (cytotoxic T-lymphocyte-associated protein 4), also known as CD152 (cluster of differentiation 152), is a protein receptor that, functioning as an immune checkpoint, downregulates immune responses. CTLA4 is constitutively expressed in Tregs but only upregulated in conventional T cells after activation. It acts as an

HVEM is found on the surface of various cell types, including hematopoietic and non-hematopoietic cells, and is expressed mainly in spleen, thymus, bone marrow, lung and intestines. It has been identified as a canonical TNF receptor, signaling through the TNF receptor-associated factors (TRAFs) leading to NFκB activation. Furthermore, in addition to acting as a signaling receptor, in binding to Ig superfamily members it acts as a ligand for these inhibitory receptors. Therefore, bidirectional signaling is possible for the HVEM-mediated signaling network, which can be involved in positive or negative immunological reactions under different contexts.

Programmed cell death protein 1, also known as PD-1 and CD279 (cluster of differentiation 279), is a protein that in humans is encoded by the PDCD1 gene. PD-1, functioning as an immune checkpoint, plays an important role in down regulating the immune system by preventing the activation of T-cells, which in turn reduces autoimmunity and promotes self-tolerance. The inhibitory effect of PD-1 is accomplished through a dual mechanism of promoting apoptosis (programmed cell death) in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells (suppressor T cells).

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1) is a protein that in humans is encoded by the CD274 gene. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes. Supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2.

Programmed cell death 1 ligand 2 (PD-L2) is a protein that is encoded by the PDCD1LG2 gene in humans. PDCD1LG2 has also been designated as CD273 (cluster of differentiation 273). Inhibitory molecules of the B7/CD28 family play a key role in the induction of immune tolerance in the tumor microenvironment. The programmed death-1 receptor (PD-1), with its ligands PD-L1 and PD-L2, constitutes an important member of these inhibitory pathways. PD-L2 expression was initially thought to be restricted to antigen-presenting cells such as macrophages and dendritic cells (DCs). However, PD-L2 expression can be induced on a wide variety of other immune cells and nonimmune cells depending on micro environmental stimuli.

V-domain Ig suppressor of T cell activation (VISTA) is a potent negative regulator of T-cell function that is expressed on hematopoietic cells. VISTA levels are heightened within the tumor microenvironment, in which its blockade can enhance antitumor immune responses in mice. In humans, blockade of the related programmed cell death 1 (PD-1) pathway has shown great potential in clinical immunotherapy trials.

CysLT1 (Cysteinyl leukotriene receptor 1) is previous named as LTD4 receptor (leukotriene D4 receptor). It is a receptor for cysteinyl leukotrienes and has highest affinity to leukotriene D4 (LTD4). The receptor mediates contraction and proliferation of smooth muscle, edema, eosinophil migration and damage to the mucus layer in the lung caused by LTD4. A CysLT1 selective antagonist, montelukast, is used clinically in the treatment of asthma.. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.

Dopamine is the predominant catecholamine neurotransmitter found in mammalian brain, where it controls a variety of functions including locomotor activity, cognition, emotion, positive reinforcement, food intake, and endocrine regulation. It also plays multiple roles in the periphery as a modulator of cardiovascular function, catecholamine release, hormone secretion, vascular tone, renal function, and gastrointestinal motility. The dopamine receptor family consists of five members, which are classified into two groups, D1-like (D1 and D5) and D2-like (D2, D3, and D4).

Dopamine is the predominant catecholamine neurotransmitter found in mammalian brain, where it controls a variety of functions including locomotor activity, cognition, emotion, positive reinforcement, food intake, and endocrine regulation. It also plays multiple roles in the periphery as a modulator of cardiovascular function, catecholamine release, hormone secretion, vascular tone, renal function, and gastrointestinal motility. The dopamine receptor family consists of five members, which are classified into two groups, D1-like (D1 and D5) and D2-like (D2, D3, and D4). Dopamine receptor 2 is mainly expressed in the brain. It has splicing variants, D2L and D2S. D2R receptor is implicated in a number of neurological and psychiatric conditions. Drugs acting at dopamine D2 receptors (D2R) are commonly used to alleviate symptoms for Parkinson’s disease, schizophrenia, and depression.

The short form of D2 (D2S) and the long form (D2L) are two isoforms that contribute differentially to dopamine signaling in both prefrontal cortex and striatum. The D2 dopamine receptor, short form (D2s) has been shown to stimulate phospholipase D (PLD) activity independent of the activation of phospholipase C (PLC) activity in GH4 derived cells stably transfected with the D2s receptor. Agonist activation of D2s has been shown to mediate the inhibition of growth in the same cell line.

Dopamine is the predominant catecholamine neurotransmitter found in mammalian brain, where it controls a variety of functions including locomotor activity, cognition, emotion, positive reinforcement, food intake, and endocrine regulation. It also plays multiple roles in the periphery as a modulator of cardiovascular function, catecholamine release, hormone secretion, vascular tone, renal function, and gastrointestinal motility. The dopamine receptor family consists of five members, which are classified into two groups, D1-like (D1 and D5) and D2-like (D2, D3, and D4). D5 receptor has a 10-fold higher affinity for dopamine than the D1 receptor.

DP1 is a G_s-coupled GPCR expressed in the colon, eye, platelets, eosinophils, that bind to PGD2 and PGE2. DP1 can inhibit platelet aggregation, and also inhibit leukotriene B4 and superoxide anion (O2-) release from human neutrophils. It can relax smooth muscle and regulate eosinophil apoptosis. DP receptor knockout OVA-challenged mice exhibit reduced Th2 cytokine levels and lymphocyte accumulation in the lung. In addition, they failed to produce asthmatic responses.

Prostaglandin D(2) (PGD(2)) is derived from arachidonic acid and binds with high affinity to the G-protein coupled receptors prostanoid DP(1) and DP(2). Interaction with DP(2) results in cell chemotaxis, eosinophil degranulation, eosinophil shape change, adhesion molecule upregulation and Th2 cytokine production. In allergic rhinitis and allergic asthma PGD(2) is released from mast cells in response to allergen challenge and may trigger symptoms such as sneezing, rhinorrhea, pruritus, mucus hypersecretion and pulmonary inflammation. GenScript’s cloned human DP2-expressing cell line co-expressing Gα15 is made in the CHO-K1 host.

In mammals, the endothelin (ET) family comprises three endogenous isoforms: ET-1, ET-2, and ET-3. These endothelium-derived peptides perform their functions via two endothelin receptors, classified as EDNRA and EDNRB. EDNRA receptors are mainly localized in the vascular smooth muscle cells, where they are the predominant sub-type, and mediate vasoconstriction and proliferation. Selective EDNRA antagonists are effective in the treatment of heart failure, essential hypertension, pulmonary hypertension, and atherosclerosis.

In mammals, the endothelin (ET) family comprises three endogenous isoforms: ET-1, ET-2, and ET-3. These endothelium-derived peptides perform their functions via two endothelin receptors, classified as EDNRA and EDNRB. EDNRB receptors present on the endothelial cells lining the vessel wall and play a role in the release of endothelium-derived relaxing factors such as nitric oxide (NO) and prostanoids and in removing ET from the circulation.

Prostaglandin (PG) E2 exerts its actions by acting on a group of G-protein-coupled receptors (GPCRs). There are four GPCRs responding to PGE2 designated subtypes EP1, EP2, EP3, and EP4 and multiple splicing isoforms of the subtype EP3. The EP subtypes exhibit differences in signal transduction, tissue localization, and expression regulation. Studies have identified that EP2 mediates many processes, such as facilitating ovulation and fertilization, suppressing dendritic cell differentiation, and promoting amyloid-β formation in Alzheimer’s disease.

Recombinant CHO-K1 cells stably overexpress human neonatal Fc receptor (FcRn) and beta-2 microglobulin (B2M). The existence of B2M enables the stable expression of FcRn. The surface expression of FcRn is validated by FACS analysis. This stable cell line product is designed for measuring binding affinity and stability of Fc region of antibodies, Fc fusion proteins, and antibody based biologics that binds with FcRn during biologics research and development.

Free fatty acid G protein coupled receptor family consists of four members and plays significant roles in nutrition regulation. GPR40 and GPR120 are activated by medium and long-chain FFAs, whereas GPR41 and GPR43 can be activated by short-chain FFAs. GPR40 is preferentially expressed in pancreatic beta-cells and mediates the majority of the effects of FFAs on insulin secretion. Researches show that GPR40 is a potential therapeutic target and plays an important role in the chain of events linking obesity and type2 diabetes.

FFA2 (GPR43) is a 330-amino acid G-protein coupled receptor that binds to fatty acid. FFA2 is highly selective expressed in leukocytes, which suggests a role in the recruitment of these cell populations toward sites of bacterial infection.

The formyl peptide receptors (FPR) are a class of G protein-coupled receptors involved in chemotaxis. FPR1 is a Gi-coupled GPCR. FPR1 is expressed in the vasculature, secretory epithelial cells, neurons and other tissues. FPR is involved in host defense against bacterial infection and in the clearance of damaged cells.

Receptor activity-modifying proteins (RAMPs) are a class of protein which interact with and modulate the activities of several Class B G Protein-Coupled Receptors including the receptors for secretin, calcitonin (CT), glucagon, and vasoactive intestinal peptide (VIP).There are three distinct types of RAMPs, designated RAMP1, RAMP2, and RAMP3, each encoded by a separate gene.
Currently the function of RAMPs is divided into 2 class activities. Association of RAMPs with either the CT or CALCRL proteins forms 6 different receptors from the calcitonin receptor family. When associated with the Calcitonin receptor (CTR) or Calcitonin receptor-like (CALCRL) RAMPs can change the selectivity of the receptor for a specific hormone. In the cases of the other receptors mentioned however, there is no evidence that they can do this, but instead function to regulate trafficking of receptors from the ER / golgi to the membrane.
GenScript’s cloned human AMY3–expressing cell line is generated in the CHO-K1/Gα15 host.

The neuropeptide galanin elicits a range of biological effects by interacting with specific G-protein-coupled receptors. Galanin receptors are seven-transmembrane proteins that have been shown to activate a variety of intracellular second-messenger pathways. GALR1 inhibits adenylyl cyclase via a G protein of the Gi/Go family. GALR1 is widely expressed in the brain, spinal cord, and peripheral sites including small intestine and heart.

Actions of neuropeptide galanin are mediated by three G-protein coupled receptors, GalR1, GalR2, and GalR3. Human GALR2 was shown to couple to phospholipase C and to be involved in the elevation of intracellular calcium levels. GALR2 mRNA shows a wide distribution in the brain (mammillary nuclei, dentate gyrus, cingulate gyrus, posterior hypothalamic, supraoptic, and arcuate nuclei) and restricted peripheral tissue distribution with highest mRNA levels detected in human small intestine. Galanin has been implicated in anxiety-related behaviors, cognition, analgesia, and feeding in rodents.

Glucagon regulates blood glucose via control of hepatic glycogenolysis and gluconeogenesis and via regulation of insulin release from the β cell. Pharmacological administration of glucagon increases blood glucose in normal and diabetic subjects, and produces positive inotropic and chronotropic cardiovascular effects, relaxation of smooth muscle in the gastrointestinal tract and stimulation of growth hormone secretion. The actions of glucagon are mediated via a single adenylate cyclase-coupled glucagon receptor that also couples to the phospholipase C-inositol phosphate (PLC-IP) pathway leading to Ca²⁺ release from intracellular stores.

Ghrelin, a 28-amino-acid gut peptide is secreted from the stomach. It stimulates the release of growth hormone (GH) from the pituitary through GHS-R and plays important roles in energy homeostasis. In addition, ghrelin acts directly on the central nervous system to decrease sympathetic nerve activity. Ghrelin receptors (GHSRs) are concentrated in the hypothalamus-pituitary unit and may take the role of ghrelin in memory. GHSR is distributed in peripheral tissues, including the heart, lung, liver, kidney, pancreas, stomach, small and large intestines, adipose, and immune cells, suggesting that ghrelin has multiple functions in these tissues.

Gastric inhibitory polypeptide receptor (GIPR) is a Gs-coupled GPCR which is expressed in the pancreas, stomach, small intestine, adipose tissue, adrenal cortex, pituitary, heart, testis, endothelial cells, bone, trachea, spleen, thymus, lung, kidney, thyroid, and several regions in the CNS. Its ligand GIP is secreted after meal ingestion has been shown to stimulate bone formation resulting in lower occurrences of osteoporosis. GIPR may have therapeutic potential in the treatment of type 2 diabetes and obesity.

Tumor necrosis factor receptor superfamily member 18 (TNFRSF18) also known as activation-inducible TNFR family receptor (AITR) or glucocorticoid-induced TNFR-related protein (GITR) is a protein that in humans is encoded by the TNFRSF18 gene. GITR is currently of interest to immunologists as a co-stimulatory immune checkpoint molecule.

GLP1R binds specifically the glucagon-like peptide-1 (GLP1) and has much lower affinity for related peptides such as the gastric inhibitory polypeptide and glucagon. GLP1R is known to be expressed in pancreatic beta cells. Activated GLP1R stimulates the adenylyl cyclase pathway which results in increased insulin synthesis and release of insulin. Consequently, GLP1R has been suggested as a potential target for the treatment of diabetes. GLP1R is also expressed in the brain where it is involved in the control of appetite. Furthermore, mice which over express GLP1R display improved memory and learning.

The glucagon-like peptides include glucagon, GLP-1, and GLP-2 exert diverse actions on nutrient intake, gastrointestinal motility, islet hormone secretion, cell proliferation and apoptosis, as well as nutrient absorptionand assimilation. Glucagon-like peptide (GLP)-2, a product of the proglucagon gene, is expressed in enteroendocrine cells of the small and large intestine and is trophic to the gastrointestinal mucosa. GLP-2 also inhibits gastric acid secretion and emptying and up-regulates intestinal hexose transport. GLP-2 acts via binding to a single G protein-coupled GLP-2 receptor (GLP-2R).

The gonadotropin-releasing hormone receptor (GNRHR), also known as the luteinizing hormone releasing hormone receptor (LHRHR), is a member of the seven-transmembrane, G-protein coupled receptor (GPCR) family. It is expressed on the surface of pituitary gonadotrope cells as well as lymphocytes, breast, ovary, and prostate. Upon activation, the LHRHr stimulates tyrosine phosphatase and elicits the release of LH from the pituitary. Evidence exists showing the presence of LHRH and its receptor in extrapituitary tissues as well as a role in progression of some cancers.

The gene GPBRA1 encodes G protein-coupled bile acid receptor. Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production.

GPR103 is known as an orphan G protein-coupled receptor with reported expression in brain, heart, kidney, adrenal gland, retina, and testis. GPR103 mRNA has been reported to be highly expressed in the superficial layers of the entire spinal cord and a high density of 26RFa binding sites was observed in the superficial layers of the dorsal horn. QRFP binds and activates the human GPR103, as well as mouse GPR103A and GPR103B, with nanomolar affinities in transfected cells. Therefore, the current experiments investigated the effects of QRFP administration in rats and the effects of a high fat diet on prepro-QRFP mRNA and GPR103 receptor mRNA levels. 26RFa and QRFP are endogenous ligands of GPR103. An immunohistochemical study revealed that GPR103-like immunoreactivity (LI) was observed in the superficial layers of spinal dorsal horn, that QRFP-LI was observed in the dorsal root ganglion and that intrathecal 26RFa suppressed the expression of Fos-LI induced by paw formalin injection in the superficial layers of the spinal dorsal horn.

The GPR68 is a proton-sensing receptor involved in pH homeostasis. A study revealed that in osteosarcoma cells and primary human osteoblast precursors which expression of GPR68 exhibit strong PH-dependent inositol phosphate formation.

CHO-K1/Gqi5 is a CHO-K1 cell line stably expressing the chimeric Gqi5 alpha subunit protein which a chimeric Gq protein instead of the last five carboxyl-terminal amino acids from Gi. It is used as a host cell for transfection expression of Gi/o-coupled receptors, the constitutively expressed Gqi5 protein in the cells allows many transfected receptors which normally inhibit the cAMP pathway, to couple to Gq signal transduction and mobilize intracellular calcium. The cell line carries the hygromycin B resistance gene and is resistant to hygromycin B.

Recombinant CHO-K1 cells stably overexpress G15 alpha subunit protein (Gα15), which belongs to Gq/11/14/15 alpha subunit family. When Gα15 and Gs-coupled or Gi/o-coupled receptor are co-expressed in cells, the cells not only can be triggered to stimulate or inhibit the cAMP pathway based on the coupled G alpha subunit types, but also can conduct Gq-coupled signal transduction and mobilize intracellular calcium following certain ligand binding. This cell line is recommended to use as a host cell line for transient or stable expression of Gs and Gi/o -coupled receptors, which is able to provide more readouts to study G protein-coupled receptors.

Receptor activity-modifying proteins (RAMPs) are a class of protein which interact with and modulate the activities of several Class B G Protein-Coupled Receptors including the receptors for secretin, calcitonin (CT), glucagon, and vasoactive intestinal peptide (VIP).There are three distinct types of RAMPs, designated RAMP1, RAMP2, and RAMP3, each encoded by a separate gene.
Currently the function of RAMPs is divided into 2 class activities. Association of RAMPs with either the CT or CALCRL proteins forms 6 different receptors from the calcitonin receptor family. When associated with the Calcitonin receptor (CTR) or Calcitonin receptor-like (CALCRL), RAMPs can change the selectivity of the receptor for a specific hormone. In the cases of the other receptors mentioned however, there is no evidence that they can do this, but instead function to regulate trafficking of receptors from the ER / golgi to the membrane.
GenScript’s cloned human AMY1–expressing cell line is generated in the CHO-K1/Gα15 host.

Receptor activity-modifying proteins (RAMPs) are a class of protein which interact with and modulate the activities of several Class B G Protein-Coupled Receptors including the receptors for secretin, calcitonin (CT), glucagon, and vasoactive intestinal peptide (VIP).There are three distinct types of RAMPs, designated RAMP1, RAMP2, and RAMP3, each encoded by a separate gene.
Currently the function of RAMPs is divided into 2 class activities. Association of RAMPs with either the CT or CALCR proteins forms 6 different receptors from the calcitonin receptor family. When associated with the Calcitonin receptor (CTR) or Calcitonin receptor-like (CALCRL) RAMPs can change the selectivity of the receptor for a specific hormone. In the cases of the other receptors mentioned however, there is no evidence that they can do this, but instead function to regulate trafficking of receptors from the ER / golgi to the membrane.
GenScript’s cloned human AMY2 (RAMP2 + CALCR)–expressing cell line is generated in the CHO-K1/Gα15 host.

C-C chemokine receptor type 1 (CCR1) is a G protein-coupled receptor member of the CC chemokine subfamily of receptors. Following interaction with its specific chemokine ligands, like macrophage inflammatory protein 1 alpha (MIP-1 alpha), regulated on activation normal T expressed and secreted protein (RANTES), and monocyte chemoattractant protein 3 (MCP-3), it triggers the onset of a process known as chemotaxis. GenScript’s human CCR1-expressing stable subline is guaranteed to function properly in the calcium flux assay.

C-C chemokine receptor type 5 (CCR5) is a G protein-coupled receptor and a co-receptor for the entry of human immunodeficiency virus-1 (HIV-1) into cells. CCR5 chemokine receptor is involved in leucocytes chemotaxis to sites of inflammation and plays an important role in the macrophages, T cells, and monocytes recruitment. The chemokine ligands that bind to CCR5 are regulated on activation, normal T Cell expressed and secreted (RANTES) and macrophage inflammatory protein 1 alpha (MIP1α). GenScript’s human CCR5-expressing stable subline is guaranteed to function properly in the calcium flux assay.