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.

Human

P2Y receptors are one of three families of extracellular receptors for purine and pyrimidine nucleotides involved in purinergic signaling. In heterologous expression systems, recombinant P2Y1, P2Y2, P2Y4, P2Y6 receptors couple to G proteins (mainly Gq) which, in turn, activate intracellular signaling cascades - mainly the phospholipase Cβ (PLCβ) isoform to mobilise intracellular Ca2+ ions. RT-PCR and Northern Blotting studies show a high expression of this receptor in spleen and placenta, followed by kidney, adipose, bone, lung, heart, brain and skeletal muscle. In mouse bone marrow-derived mast cells (mBMMCs) and in the human MC line LAD2, P2Y6 receptors cooperate with CysLT1R to promote cell survival and chemokine generation by a pathway involving reciprocal ligand-mediated cross-talk. In human, rat and mouse, P2Y6 expression is increased by the stress associated with intestinal inflammation, leading to the release of CXC chemokine ligand 8. In rabbit, the receptor functions by increasing osteoclast survival through the NFκB pathway.

Human

The neuropeptide S receptor isoform a (NPS1a) is Gq/11 and Gs-coupled GPCRs expressed in the bronchial smooth muscle cells, basally in colon epithelium and in occasional basal keratinocytes in skin. An Asn107->Ile mutation is significantly up-regulated in a mouse model of ovalbumen-induced lung inflammation supporting a role in the pathogenesis of asthma.

Human

The thromboxane A2 (TxA2) receptor (TP) is a member of the G protein-coupled receptor (GPCR) superfamily which mediates TxA2-induced platelet aggregation and vasoconstriction. Dysregulation of TxA2 synthesis and function has been implicated in the pathogenesis of a number of disease states including myocardial ischemia, asthma, pregnancy-induced hypertension, and a variety of kidney diseases. TP receptors (Thromboxane A2 receptors) are widely distributed among different organ systems and localized on both cell membranes and in intracellular structures. Two isoforms of human TPs have been cloned from placenta (TPα) and endothelium (TPβ) that differ in their mechanisms and kinetics of desensitization and internalization. The TPs are linked via the Gq/G11 class of G proteins to phospholipase C (PLC), which hydrolyzes phosphoinositides to two potent second messengers: inositol 1,4,5-trisphosphate, which leads to an increase in cytoplasmic free calcium, and diacylglycerol (DAG), which activates protein kinase C (PKC).

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.

Human

Muscarinic acetylcholine receptors belong to a superfamily of seven-TM-domain receptors that interact with G-proteins to initiate intracellular responses. Five muscarinic receptor subtypes have been identified and named from M1 to M5. The M4 muscarinic receptor couples to Gi/o to inhibit cAMP production. GenScript co-transfected human M4 with Gα15 in the CHO-K1 which supports high levels of recombinant M4 expression on the cell surface and contains high levels of Gα15 to couple the receptor to the calcium signaling pathway.

Human

The orexin/hypocretin peptides orexin A and orexin B (also known as hcrt-1 and hcrt-2) are 33- and 28-amino acid peptides, respectively. They are preferentially expressed in hypothalamus. The orexins have a range of physiological functions including feeding control, energy metabolism, neuroendocrine function modulation, and sleep-wake cycle regulation. The two orexin receptor subtypes OX1 and OX2 both mediate the action of orexin-A and orexin-B and couple efficiently through Gq/11 to activate phospholipase C and lead to elevation of intracellular calcium.

Human

The melanocortin receptor 5, MC5 receptor, is Gs-coupled GPCRs expressed in the adrenal gland, fat cells, kidney, leukocytes, lung, lymph node, mammary gland, ovary, pituitary, testis and uterus. Mice with targeted deletion of the MC5 receptor have a defect in water and thermoregulation secondary to their decreased production of sebaceous lipids.

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.

Human

Muscarinic acetylcholine receptors belong to a superfamily of seven-TM-domain receptors that interact with G-proteins to initiate intracellular responses. Five muscarinic receptor subtypes have been identified and named from M1 to M5. The M3 muscarinic receptors are located at many places in the body, e.g. smooth muscles, endocrine, exocrine glands, as well as lungs. They are also found in the CNS, where it induces emesis. They generally cause smooth muscle contraction and increased glandular secretions.