IFN-gamma R1/CD119 Protein, Human (HEK293, His-Flag)

IFN-γ R1/CD119 is an important receptor subunit of interferon γ/INFG that activates effector immune cells and enhances antigen presentation, contributing to antibacterial, antiviral, and antitumor responses. It cooperates with IFNGR2 to form a functional receptor. IFN-gamma R1/CD119 Protein, Human (HEK293, His-Flag) is the recombinant human-derived IFN-gamma R1/CD119 protein, expressed by HEK293 , with C-6*His, C-Flag labeled tag.

IFN-gamma R1 (CD119) serves as the receptor subunit for interferon gamma (IFNG), playing pivotal roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Teaming up with the transmembrane accessory factor IFNGR2, IFNGR1 forms a functional receptor complex. Upon IFNG binding, the intracellular domain of IFNGR1 undergoes conformational changes, allowing the association of downstream signaling components, including JAK1 and JAK2. Activated JAK1 phosphorylates IFNGR1, creating a docking site for STAT1. Subsequent phosphorylation of STAT1 leads to dimerization, translocation to the nucleus, and stimulation of target gene transcription. IFNGR1 also facilitates the activation of STAT3, albeit to a lesser extent. Furthermore, the phosphorylated IFNGR1 domain provides a docking site for SOCS1, which regulates the JAK-STAT pathway by competing with STAT1 for binding to IFNGR1. IFNGR1 can exist as a monomer and forms a heterodimer with IFNGR2 to constitute the IFNG receptor complex. The receptor also interacts with JAK1, STAT1, and SOCS1, orchestrating a complex signaling network in response to IFNG.

Human

HEK293

C-6*His;C-Flag

P15260-1 (E18-G245)

3459  [NCBI]

EMGTADLGPSSVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDACINISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKG

29 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.