{"product_id":"human-ifn-protein-bhp13700075","title":"Human IFN-? protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFN-Γ\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG; IFI; IFN gamma; Interferon Gamma; Interferon gamma; IFNG.\u003c\/p\u003e\u003cp\u003eHuman IFN-γ protein, expressed in CHO Stable Cells\u003c\/p\u003e\u003cp\u003eIFN-γ, also known as IFNG, is a secreted protein which belongs to the type I I interferon family. IFN-γ is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN-γ has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN-γ is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN-γ expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN-γ in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIFN-Γ\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eInfectious Disease\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 16.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The secreted recombinant human IFN-γ consists of 143 amino acids and has a predicted molecular mass of 16.7 kDa. γ-IFN migrates as two bands with apparent molecular mass of 21\u0026amp;25 kDa probably due to different glycosylation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human IFN-γ (NP_000610.2) (Met 1-Gln 166) was expressed and purified.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 92 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Mammalian expression can support native-like folding, disulfide bond formation, and glycosylation—features that are often important for secreted proteins, receptors, and adhesion molecules. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e CHO Stable Cells. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e Many recombinant proteins incorporate affinity tags (e.g., His, GST, Fc) to aid purification and capture in binding assays. Where relevant, tag status can be considered when comparing activity or interaction data.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"20 ug","offer_id":52997737283949,"sku":"PRP100263-20UG","price":129.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP100263-1.jpg?v=1770191167","url":"https:\/\/www.ebiohippo.com\/products\/human-ifn-protein-bhp13700075","provider":"BioHippo","version":"1.0","type":"link"}