Cat. No：GM-032AS007
Product：H_SIRPα/CD47 Reporter Blockade Assay(Jurkat:CHO)
Cat. No：GM-032AS007
Product：H_SIRPα/CD47 Reporter Blockade Assay(Jurkat:CHO)
H_SIRPα-CD3ζ Reporter Jurkat Cell Line
Cell Growth Medium：RPMI 1640+10% FBS+1% P.S+400 μg/mL G418+0.75 μg/mL Puromycin+200 μg/mL Hygromycin+3.5 μg/mL Blasticidin
Cell Freezing Medium：90% FBS+10% DMSO
H_CD47 CHO-K1 cell line
Cell Growth Medium：F12K+10% FBS+1% P.S+4 μg/mL Puromycin
Cell Freezing Medium：90% FBS+10% DMSO
Assay Buffer：RPMI 1640+1% FBS+1% P.S
CD47, known as Integrin-Associated Protein (IAP), is a transmembrane protein encoded by the CD47 gene in the human body. It belongs to the immunoglobulin superfamily and can interact with integrins, thrombospondin-1 (TSP-1), and signal regulatory protein alpha (Sirpα). Its protein structure includes an extracellular N-terminal IgV domain, 5 transmembrane domains, and an intracellular C-terminal transmembrane glycoprotein, expressed widely on the surface of almost all normal cells.
Sirpα is a membrane glycoprotein from the SIRP family, expressed specifically on macrophages, dendritic cells, and nerve cell surfaces. As an inhibitory receptor, Sirpα interacts with CD47, releasing a "do not eat me" signal, thus inhibiting phagocytosis by macrophages. Some tumor cells also overexpress CD47 to escape immune surveillance. The cytoplasmic region of SIRPα is highly conserved among humans, rats, and mice, containing numerous tyrosine residues in the ITIM motif. Upon binding to CD47, Sirpα becomes phosphorylated and recruits SHP1 and SHP2 to transmit intracellular signals.
The Genomeditech H_SIRPα/CD47 Reporter Blockade Assay cell line reports on gene expression. When CD47 binds to SIRPα, it activates CD3ζ, leading to the expression of luciferase. This activation can be blocked by antibodies with a blocking effect, making this cell model suitable for screening blocking antibodies. Luciferase readings reflect the activation and blocking effects of the signaling pathway, making it useful for evaluating the in vitro effects of CD47 and SIRPα-related antibody drugs.
Cat. No：GM-032AS007
Product：H_SIRPα/CD47 Reporter Blockade Assay(Jurkat:CHO)
H_SIRPα-CD3ζ Reporter Jurkat Cell Line
Cell Growth Medium：RPMI 1640+10% FBS+1% P.S+400 μg/mL G418+0.75 μg/mL Puromycin+200 μg/mL Hygromycin+3.5 μg/mL Blasticidin
Cell Freezing Medium：90% FBS+10% DMSO
H_CD47 CHO-K1 cell line
Cell Growth Medium：F12K+10% FBS+1% P.S+4 μg/mL Puromycin
Cell Freezing Medium：90% FBS+10% DMSO
Assay Buffer：RPMI 1640+1% FBS+1% P.S
CD47, known as Integrin-Associated Protein (IAP), is a transmembrane protein encoded by the CD47 gene in the human body. It belongs to the immunoglobulin superfamily and can interact with integrins, thrombospondin-1 (TSP-1), and signal regulatory protein alpha (Sirpα). Its protein structure includes an extracellular N-terminal IgV domain, 5 transmembrane domains, and an intracellular C-terminal transmembrane glycoprotein, expressed widely on the surface of almost all normal cells.
Sirpα is a membrane glycoprotein from the SIRP family, expressed specifically on macrophages, dendritic cells, and nerve cell surfaces. As an inhibitory receptor, Sirpα interacts with CD47, releasing a "do not eat me" signal, thus inhibiting phagocytosis by macrophages. Some tumor cells also overexpress CD47 to escape immune surveillance. The cytoplasmic region of SIRPα is highly conserved among humans, rats, and mice, containing numerous tyrosine residues in the ITIM motif. Upon binding to CD47, Sirpα becomes phosphorylated and recruits SHP1 and SHP2 to transmit intracellular signals.
The Genomeditech H_SIRPα/CD47 Reporter Blockade Assay cell line reports on gene expression. When CD47 binds to SIRPα, it activates CD3ζ, leading to the expression of luciferase. This activation can be blocked by antibodies with a blocking effect, making this cell model suitable for screening blocking antibodies. Luciferase readings reflect the activation and blocking effects of the signaling pathway, making it useful for evaluating the in vitro effects of CD47 and SIRPα-related antibody drugs.
