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Recombinant Human IL-12 Protein

Cat # Size Price Quantity
63010110 µg$195
630102100 µg$795

  Bulk/Custom

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)
SpeciesHuman
accession numberP29459-1 &NP_002178.2
SourcesA DNA sequence encoding the human IL12A (P29459-1)(Met1-Ser219) was expressed, constructed the plasmid 1; A DNA sequence encoding the human IL12B (NP_002178.2)(Met1-Ser328) was expressed, constructed the plasmid 2. The two plasmids were co-expressed and the human IL12A&IL12B heterodimer was purified.
Molecular WeightThe recombinant heterodimer of human IL12A&IL12B comprises 503(197+306) amino acids and has a calculated molecular mass of 57.2(22.5+34.7) KDa. The apparent molecular mass of human IL12 heterodimer is approximately 34 & 41 kDa respectively in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
Regulatory StatusRUO
Endotoxin level<0.01EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingProteins 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.
Research AreasCytokines, Inflammation, Th1 cells, NK cells, T cells, Infectious Diseases

Background Information

Human interleukin-12 (IL-12) is a proinflammatory cytokine that plays a central role in bridging innate and adaptive immunity. It is primarily produced by antigen-presenting cells such as dendritic cells, macrophages, and B cells in response to pathogens. IL-12 promotes the differentiation of naïve CD4+ T cells into T helper 1 (Th1) cells and enhances the cytotoxic activity of natural killer (NK) cells and CD8+ T lymphocytes. A key function of IL-12 is the induction of interferon-gamma (IFN-γ) production, which amplifies cellular immune responses against intracellular pathogens.


Structurally, IL-12 is a heterodimer composed of two covalently linked subunits: p35 and p40. These subunits are encoded by separate genes and must assemble to form the biologically active cytokine, often referred to as IL-12p70. IL-12 signals through a receptor complex consisting of IL-12Rβ1 and IL-12Rβ2 chains, leading to activation of the JAK-STAT signaling pathway, particularly STAT4.


In disease, dysregulated IL-12 production is associated with chronic inflammation and autoimmune conditions such as psoriasis and inflammatory bowel disease. Conversely, insufficient IL-12 activity can impair host defense against infections. Therapeutically, IL-12 has been explored as an immunostimulatory agent in cancer, aiming to boost anti-tumor immunity. However, systemic toxicity has limited its direct use, leading to alternative strategies such as targeted delivery or modulation of its signaling pathway.

Data Sheets

Recombinant Human 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.

Have a product or application question? Consult our FAQs or contact us.