金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived, Gln24-Gln166, with an N-terminal Met Accession #:CAA31639 N-terminal Sequence Analysis:Met Purity:>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin Level:< 0.01 EU per 1 μg of the protein by the LAL method. Predicted Molecular Mass:16.9 kDa SDS-PAGE:17 and 16 kDa, reducing conditions Activity:Measured in anti-viral assays using HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. 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 typically 0.15-0.75 ng/mL. Formulation:Lyophilized from a 0.2 µm filtered solution in Sodium Succinate, Mannitol and Tween^® 80. See Certificate of Analysis for details. Molecule Information: IFN-gamma Long Name: Interferon gamma Aliases: IFNG Entrez Gene IDs: 3458 (Human); 15978 (Mouse); 25712 (Rat); 396991 (Porcine); 281237 (Bovine); 403801 (Canine); 493965 (Feline) Background: IFN-gamma View IFN gamma IHC images.

Interferon-γ (IFN-γ, also known as Type II interferon or immune interferon) is a cytokine produced primarily by T-lymphocytes and natural killer cells. The protein shares no significant homology with IFN-β or the various IFN-α family proteins. Mature IFN-γ exists as noncovalently-linked homodimers. Human IFN-γ is highly species specific and is biologically active only in human and primate cells.

IFN-γ was originally characterized based on its antiviral activities. The protein also exerts anti-proliferative, immunoregulatory and proinflammatory activities and is thus important in host defense mechanisms. IFN-γ induces the production of cytokines, up-regulates the expression of class I and II MHC antigens, Fc receptor and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching and potentiates the secretion of immunoglobulins by B cells. IFN-γ also augments Helper T cell expansion and may be required for Helper T cell differentiation.

IFN-γ exerts its biological activities by binding to specific cell surface receptors with high-affinity binding sites. The IFN-γ receptor is present on almost all cell types except mature erythrocytes and has been cloned and characterized. The IFN-γ receptor is structurally related to the IL-10 receptor.