Recombinant human IL-17E (Fc tag) Protein

Cat # Size Price Quantity
63220150 μg$330
632202500 μg$1250

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameIL-25, IL-17E
SpeciesHuman
accession numberNP_073626.1)
SourcesA DNA sequence encoding the mature form of human IL25 (Tyr 33-Gly177) (NP_073626.1) was fused with the Fc region of human IgG1 at the N-terminus via a polypeptide linker.
Molecular WeightThe recombinant human IL25/Fc chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 425 amino acids and predicts a molecular mass of 47.55 KDa. As a result of glycosylation, the apparent molecular mass of rh IL25/Fc monomer is approximately 50-60 KDa in SDS-PAGE under reducing conditions.
Affinity TagN-hFc
Purity> 95 % 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


Interleukin-25 (IL-25), also known as IL-17E, is a member of the IL-17 cytokine family that plays a pivotal role in initiating and amplifying type 2 immune responses. Unlike other IL-17 family members that primarily promote neutrophilic inflammation, IL-25 drives the production of Th2-associated cytokines, including IL-4, IL-5, and IL-13. It is produced by epithelial cells, tuft cells, mast cells, eosinophils, basophils, macrophages, and activated T cells in response to allergens, parasites, and tissue injury, thereby contributing to host defense against helminth infections while also promoting allergic inflammation.

Human IL-25 is a secreted glycoprotein consisting of 177 amino acids and adopts the characteristic cystine-knot fold shared by IL-17 family cytokines. IL-25 functions as a homodimer and signals by binding to a heterodimeric receptor complex composed of IL-17RB (IL-25R) and IL-17RA. Receptor engagement activates adaptor proteins such as Act1, leading to NF-κB, MAPK, and JAK/STAT signaling pathways that stimulate the expression of type 2 inflammatory mediators.

IL-25 has been implicated in numerous inflammatory and immune-mediated diseases, including asthma, allergic rhinitis, atopic dermatitis, chronic rhinosinusitis with nasal polyps, eosinophilic esophagitis, and inflammatory bowel disease. Elevated IL-25 expression contributes to eosinophilic inflammation, mucus hypersecretion, airway remodeling, and enhanced IgE production. In cancer, IL-25 exhibits context-dependent effects, with studies suggesting both anti-tumor immune activation and tumor-promoting activities depending on the tumor type and microenvironment.

Given its central role in type 2 immunity, the IL-25/IL-17RB signaling axis has emerged as a promising therapeutic target. Experimental monoclonal antibodies targeting IL-25 or IL-17RB have demonstrated efficacy in preclinical models of allergic asthma and other eosinophilic disorders. Although no IL-25-targeted therapies have yet received regulatory approval, ongoing research suggests that selective inhibition of IL-25 signaling may provide a novel approach for treating allergic, inflammatory, and fibrotic diseases while complementing existing biologic therapies directed against IL-4, IL-5, IL-13, and TSLP.

Data Sheets


Recombinant human IL-17E (Fc tag) 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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