Recombinant Mouse IL-12 Protein

Cat # Size Price Quantity
67120120 μg$330
67120250 μg$700

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameIL-12, Natural killer cell stimulatory factor (NKSF), cytotoxic lymphocyte maturation factor (CLMF)
SpeciesMouse
accession numberP43431 & P43432
SourcesA DNA sequence encoding the p35 subunit of mouse IL12, termed as IL12A (P43431) (Met 1-Ala 215) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 1; A DNA sequence encoding the p40 subunit of mouse IL12, termed as IL12B (P43432) (Met 1-Ser 335) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 2. The two plasmids were co-expressed and the heterodimer was purified.
Molecular WeightThe recombinant mouse IL12 heterodimer of IL12A/IL12B, comprises 528 (204 + 324) amino acids and has a calculated molecular mass of 60.3 (23.1 + 37.2) KDa. The apparent molecular mass of IL12 heterodimer is approximately 28 & 47 KDa respectively in SDS-PAGE under reducing conditions.
Affinity TagC-His
Purity≥90% as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 1.0 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information


Mouse interleukin-12 (IL-12) is a pro-inflammatory cytokine that plays a central role in cell-mediated immunity by promoting T-helper 1 (Th1) cell differentiation, activating natural killer (NK) cells, and enhancing the production of interferon-gamma (IFN-γ). It is produced primarily by activated dendritic cells, macrophages, and other antigen-presenting cells in response to microbial components and immune stimuli. Through these activities, IL-12 helps coordinate innate and adaptive immune responses against intracellular pathogens and contributes to antitumor immunity.



Mouse IL-12, also known as IL-12p70, is a heterodimeric protein composed of two disulfide-linked subunits: p35 (encoded by Il12a) and p40 (encoded by Il12b). The p40 subunit is also shared with IL-23, in which it pairs with the p19 subunit. IL-12 signals through a heterodimeric receptor consisting of IL-12Rβ1 and IL-12Rβ2. Receptor engagement activates Janus kinases, particularly TYK2 and JAK2, leading primarily to STAT4 activation and increased IFN-γ production. Unlike some cytokines, IL-12 does not have a conventional soluble ligand; instead, its biological activity depends on binding to its specific cell-surface receptor.



IL-12 is important in host defense against intracellular bacteria, parasites, and certain viruses. Impaired IL-12 signaling can weaken cellular immunity and increase susceptibility to some infections. Conversely, excessive IL-12 activity may contribute to chronic inflammation, autoimmune conditions, and tissue damage by sustaining Th1 responses and inflammatory cytokine production. Its effects depend on the infection, tissue environment, and balance of other immune mediators.



Because IL-12 can stimulate cytotoxic T cells and NK cells, it has been investigated as an immunotherapeutic agent for cancer. Experimental approaches include recombinant IL-12, localized IL-12 delivery, and engineered immune cells expressing IL-12 to enhance antitumor activity while limiting systemic toxicity. Mouse IL-12 is widely used in preclinical research to investigate Th1 immunity, cytokine signaling, infectious disease, inflammatory disorders, and cancer immunotherapy.

Data Sheets


Recombinant Mouse IL-12 Protein TDS

Frequently Asked Questions


What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.

What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.

How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.

Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.

Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

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