Recombinant Human IL-5 Protein

Cat # Size Price Quantity
6338015 μg$65
633802100 μg$600

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH7.4.
Expression HostE.coli
Target NameIL-5, Interleukin 5, B-cell differentiation factor I, T-cell replacing factor
SpeciesHuman
accession numberP05113
SourcesA DNA sequence encoding the human IL5 (P05113) (Ile20-Ser134) was expressed.
Molecular WeightThe recombinant human IL5 consists of 115 amino acids and predicts a molecular mass of 13.1 KDa.
Affinity TagNone
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


Human interleukin-5 (IL-5) is a hematopoietic cytokine that plays a central role in the growth, differentiation, survival, and activation of eosinophils. It is produced primarily by type 2 helper T cells (Th2 cells), group 2 innate lymphoid cells (ILC2s), and other immune cell populations during type 2 immune responses. IL-5 supports eosinophil development in the bone marrow, promotes their release into circulation, and enhances their recruitment and activation at sites of inflammation. It also contributes to B-cell growth and antibody production under certain conditions.



Human IL-5 is a secreted glycoprotein belonging to the four-helix bundle family of class I cytokines. The mature protein contains approximately 115 amino acids per subunit and forms a biologically active homodimer stabilized by interchain disulfide bonds. Its structure supports receptor binding and biological activity. Unlike membrane-bound signaling molecules, IL-5 functions as a soluble ligand that engages a specific cell-surface receptor complex.



The IL-5 receptor consists of an IL-5-specific alpha subunit (IL-5Rα/CD125) and a common beta subunit (βc/CD131), which is shared with the receptors for interleukin-3 and granulocyte-macrophage colony-stimulating factor (GM-CSF). IL-5 binding promotes assembly or rearrangement of the receptor complex and activates intracellular signaling pathways, including JAK/STAT, MAPK, and PI3K pathways. These signals regulate eosinophil proliferation, survival, differentiation, and effector functions.



Dysregulated IL-5 signaling contributes to eosinophilic inflammation and is strongly associated with asthma, particularly eosinophilic asthma, as well as eosinophilic granulomatosis with polyangiitis and hypereosinophilic syndromes. Excessive eosinophil accumulation can damage tissues through the release of cytotoxic granule proteins and inflammatory mediators. Therapeutically, IL-5 is an important target for biologic treatments. Mepolizumab and reslizumab neutralize IL-5, whereas benralizumab targets IL-5Rα and promotes eosinophil depletion. These therapies can reduce eosinophilic inflammation, decrease asthma exacerbations, and improve disease control in appropriately selected patients.

Data Sheets


Recombinant Human IL-5 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.