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Recombinant Mouse IL-4 Protein

Cat # Size Price Quantity
6704015 μg$65
670402100 μg$550

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostE.coli
Target NameIL-4,interleukin-4, B cell growth factor 1 (BCGF-1), B-cell stimulatory factor 1 (BSF-1), lymphocyte stimulatory factor 1,
SpeciesMouse
accession numberNP_067258.1
SourcesA DNA sequence encoding the mouse IL4 (NP_067258.1) (His23-Ser140) was expressed with a N-terminal Met.
Molecular WeightThe recombinant mouse IL4 consists of 119 amino acids and predicts a molecular mass of 13.4 KDa. It migrates as an approximately 14 KDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
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-4 (IL-4) is a pleiotropic cytokine that plays a central role in type 2 immunity, allergic inflammation, and immune-cell differentiation. It is produced primarily by activated T helper 2 (Th2) cells, as well as mast cells, basophils, eosinophils, and other immune-cell populations under appropriate conditions. IL-4 promotes the differentiation of naïve CD4+ T cells into Th2 cells, supports B-cell proliferation and antibody class switching to IgG1 and IgE in mice, and influences macrophage polarization toward an alternatively activated, M2-like phenotype. These activities contribute to parasite defense, tissue repair, and regulation of inflammatory responses.



Mouse IL-4 is a secreted cytokine belonging to the type I cytokine family. Its mature protein is approximately 120 amino acids long and adopts a characteristic four-alpha-helix bundle structure. IL-4 signals through two receptor complexes: the type I receptor, composed of IL-4 receptor alpha (IL-4Rα) and the common gamma chain (γc/CD132), and the type II receptor, composed of IL-4Rα and IL-13 receptor alpha 1 (IL-13Rα1). IL-4 binds IL-4Rα as its primary receptor-binding component, enabling recruitment of the second receptor chain and activation of intracellular signaling, particularly the JAK–STAT6 pathway.



Dysregulated IL-4 signaling contributes to allergic diseases, including asthma, atopic dermatitis, and food allergy, by promoting IgE production, Th2 responses, and mucus-associated inflammation. Excessive type 2 immunity may also contribute to fibrosis and certain tumor-associated immune environments. Conversely, IL-4 supports protective responses against helminth parasites and can promote tissue repair.



Therapeutically, IL-4 signaling is an important target in allergic and inflammatory disease. Blocking IL-4Rα can inhibit signaling by both IL-4 and IL-13, reducing type 2 inflammation. Mouse IL-4 is widely used in preclinical research to investigate Th2 differentiation, macrophage biology, allergic disease mechanisms, and potential immunomodulatory therapies.

Data Sheets

Recombinant Mouse IL-4 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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