IFN-γ (human, recombinant)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • IFNγ Th 1 CD 8+ IL12 IL18 IL4 IL10 TGFγ gluco corticoids anti viral bacterial IFNGR
• Product Overview:
  Interferon γ (IFN-γ) is a cytokine and type II interferon with roles in innate and adaptive immunity.{23537} It is initially produced by natural killer (NK) and natural killer T (NKT) cells as part of the innate immune response to pathogens, and then by CD4+ T helper (Th1) cells and CD8+ cytotoxic effector T cells as adaptive antigen-specific immunity is developed.{23537,55203} IFN-γ production is induced in response to pathogen-induced secretion of IL-12 and IL-18 by macrophages and is inhibited by IL-4, IL-10, TGF-β, and various glucocorticoids. It facilitates amplification of antigen presentation, the production of reactive oxygen species (ROS), and the induction of antiviral and antibacterial responses by binding to the interferon γ receptor extracellular domain IFNGR1 (Item No. 32006) to induce signal transduction and gene transcription.{23537,52202} In addition to its role in infectious disease, IFN-γ enhances the antigenicity of tumor cells, making them more susceptible to IFN-γ-stimulated immune effector cells.{55205} It induces tumor cell apoptosis and necroptosis, and inhibits tumor angiogenesis in vitro and in vivo. However, IFN-γ-induced removal of highly antigenic tumor cells can leave behind a population with reduced immunogenicity that can evade immune detection and enhance metastasis. Knockdown of Ifng improves insulin resistance in a mouse model of high-fat diet-induced obesity and increases susceptibility to various pathogens in mice.{23537,55204} Cayman’s IFN-γ (human, recombinant) protein can be used for cell-based assay applications. The protein consists of 143 amino acids, has a calculated molecular weight of 16.7 kDa, and a predicted N-terminus of Gln24 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, Cayman’s IFN-γ (human, recombinant) migrates as two bands at 21 and 25 kDa due to apparent differential glycosylation.