Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit rhIFN-gamma mediated protection of HeLa human cervical epithelial carcinoma cells to viral lysis. Meager, A. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 129. The ED50 for this effect is 1-3 µg/mL in the presence of 2 ng/mL rhIFN-gamma . |
Source | Mouse myeloma cell line, NS0-derived human IFN-gamma R1/CD119 protein Met1-Gly245 |
Accession # | |
N-terminal Sequence | Glu18 & Gly20 |
Protein/Peptide Type | Recombinant Proteins |
Gene | IFNGR1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 25 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 40 kDa and 50 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile PBS. |
The high-affinity IFN-gamma receptor complex is made up of two type I membrane proteins, IFN-gamma R1 (IFN‑ gamma R alpha ) and IFN-gamma R2 (IFN-gamma R beta ). Both proteins are members of the type II cytokine receptor family and share approximately 52% overall sequence identity. IFN-gamma R1 is the ligand-binding subunit that is necessary and sufficient for IFN-gamma binding and receptor internalization. IFN-gamma R2 is required for IFN‑ gamma signaling but does not bind IFN-gamma by itself. Human IFN-gamma R1 cDNA encodes a 499 amino acid (aa) residue protein with a 17 aa signal peptide, a 228 aa extracellular domain, a 23 aa transmembrane domain, and a 221 aa intracellular domain. Human and mouse IFN-gamma R1 share 52% amino acid sequence similarity and bind IFN-gamma in a species‑specific manner. IFN-gamma R1 is constitutively expressed in most cell types. Soluble IFN-gamma R1 that binds IFN-gamma has been detected in biological fluids. The recombinant soluble IFN-gamma R1 produced at R&D Systems has been shown to bind IFN-gamma with high affinity and is a potent IFN-gamma antagonist.
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