Recombinant human IL-33 Protein

Cat # Size Price Quantity
6321015 μg$100
632102100 μg$780

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostE.coli
Target NameIL-33, IL-1F11
SpeciesHuman
accession numberNP_254274.1
SourcesA DNA sequence encoding the C-terminal segment of human IL33 (NP_254274.1) (Ser 112-Thr 270) was expressed with an initial Met at the N-terminus.
Molecular WeightThe recombinant human IL33 comprises 160 amino acids and predicts a molecular mass of 18 kDa as estimated in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC. ≥ 90 % as determined by SEC-MALS(Routinely tested).
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-33 (IL-33) is a member of the interleukin-1 (IL-1) cytokine family and functions as both a cytokine and an intracellular nuclear factor. It is constitutively expressed by epithelial cells, endothelial cells, fibroblasts, and other structural cells, where it serves as an "alarmin" that is rapidly released following tissue injury or cellular stress. Once released, IL-33 alerts the immune system to tissue damage and promotes both innate and adaptive immune responses.

Human IL-33 is synthesized as a 270-amino acid precursor protein with an N-terminal nuclear localization domain and a C-terminal IL-1-like cytokine domain. Unlike many cytokines, full-length IL-33 is biologically active, although its activity can be modified by proteolytic processing. Its primary receptor is ST2 (IL1RL1), which forms a signaling complex with the co-receptor IL-1 receptor accessory protein (IL-1RAcP). Binding of IL-33 to ST2 activates MyD88-dependent signaling pathways, leading to NF-κB and MAP kinase activation and the production of inflammatory mediators.

IL-33 plays a central role in type 2 immune responses by activating type 2 innate lymphoid cells (ILC2s), mast cells, eosinophils, basophils, Th2 cells, and regulatory T cells. Dysregulated IL-33 signaling has been implicated in numerous diseases, including asthma, allergic rhinitis, atopic dermatitis, chronic obstructive pulmonary disease, inflammatory bowel disease, rheumatoid arthritis, cardiovascular disease, and certain cancers, where its effects may either promote anti-tumor immunity or support tumor progression depending on the tumor microenvironment.

Because of its broad involvement in inflammatory diseases, the IL-33/ST2 signaling axis has become an attractive therapeutic target. Monoclonal antibodies targeting IL-33 (such as itepekimab and tozorakimab) or its receptor ST2 are currently being evaluated in clinical trials for asthma, COPD, and other inflammatory disorders. These therapies aim to suppress excessive type 2 inflammation while preserving normal immune function, making IL-33 an important target for next-generation immunomodulatory treatments.

Data Sheets


Recombinant human IL-33 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.