Recombinant CHO-K1 cells stably overexpress human SARS-CoV-2 spike protein on their surface. The surface expression of SARS-CoV-2 spike protein is validated by FACS analysis. This stable cell line product is designed for screening antibodies against the SARS-CoV-2 spike protein, as well as measuring binding affinity and stability of antibody-based biologics that bind with spike protein. GenScript also offers spike protein expressing HEK293T stable cell line (Cat. No. M00804) for SARS-CoV-2 study.

Human

Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and are subsets of T cells. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response.

Recombinant HEK293T cells stably overexpress coronavirus SARS-CoV-2 spike protein on the surface. The surface expression of SARS-CoV-2 spike protein is validated by FACS analysis. This stable cell line product is designed for screening antibodies against SARS-CoV-2 spike protein, as well as for measuring binding affinity and stability of antibody based biologics that bind with spike protein. GenScript also offers spike protein expressing CHO-K1 stable cell line (Cat. No. M00803) for SARS-CoV-2 study.

Recombinant CHO-K1 cells stably overexpress human G protein subunit alpha 15 (Gα15) in the cytoplasm. This protein enables G protein-coupled receptor binding activity and acts upstream of or within with a positive effect on calcium-mediated signaling.

Recombinant CHO-K1 cells stably overexpress human mas-related G-protein coupled receptor member X2 (MRGPRX2) on the surface and contain high levels of G protein Gαq and Gαi to couple with the receptor in downstream signaling pathways.

Recombinant CHO-K1 cells stably overexpress human receptor activity modifying protein 1 (RAMP1) and calcitonin receptor (CTR) on the surface. Amylin receptors (AMYR) are a class of special protein heterodimers, composed of a CTR combined with one of three homologous receptor activity-modifying proteins (RAMP1, RAMP2, RAMP3), forming three subtypes (AMY1, AMY2, AMY3). This cell contain high levels of G protein Gαs to couple with the receptor in downstream signaling pathways.

HEK293/Gα15 is a HEK293 cell line stably expressing the Gα15 alpha subunit protein which a Gq protein.  It is used as a host cell for transfection expression of Gs and Gi/o -coupled receptors, the constitutively expressed Gα15 protein in the cells allows many transfected receptors which normally stimulate/inhibit the cAMP pathway, to couple to Gq signal transduction and mobilize intracellular calcium.  The cell line carries the puromycin resistance gene and is resistant to puromycin

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.

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.

Human

Cluster of Differentiation 112 (CD112), also known as poliovirus receptor related protein 2 (PVRL2 or PRR2), is a single-pass type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. CD112 protein also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and thus is involved in cell to cell spreading of these viruses. CD112 protein has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226/CD112 protein can induce NK cell- and CD8+ T cell-mediated cytotoxicity and cytokine secretion. CD112 has been regarded as a critical component in allergic reactions, and accordingly may function as a novel target for anti-allergic therapy.

cyno

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

Human

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.