| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | Mouse IFN-γ protein、IFN-γ |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Shipping | |
| Species | |
| Storage | |
| Target |
Background
IFN-Γ is supplied as a recombinant protein reagent for research use only. 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.
Also known as: Mouse IFN-γ protein、IFN-γ.
Species origin: Mouse.
IFN gamma (IFN-γ), also known as IFNG, is a secreted protein which belongs to the type I I interferon family. IFN gamma 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 gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN gamma expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN gamma 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.
Endotoxin: <1 EU per μg of the protein by the LAL method
Biological significance and function
Functionally, IFN-Γ 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 Immunology & Inflammation.
Molecular characteristics
Molecular characteristics: 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.
- Source species: Mouse
- Molecular weight: 16.9 kDa
- Protein length: The recombinant Mouse IFN-γ protein consists of 154 amino acids and predicts a molecular mass of 16.9 kDa.
- Expression region: Amino acid sequence derived from Mouse IFN-γ protein soluble form (NP_P01580) (His23-Cys155) was expressed, was expressed with a polyhistidine tag at the N-terminus.
- Purity: > 95 % as determined by SDS-PAGE
- Biological activity: Measured in a cell proliferation assay using L929. The ED50 for this effect is typically 0.03 ng/mL. The specific activity of recombinant Mouse IFN-γ is approximately >3.33 x 107IU/mg.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.
Expression and purification strategy
Expression system: E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Lyophilized from sterile 150 mM NaCl 20 mM Tris , pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: 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.
