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Recombinant Human IL-1β Protein

Cat # Size Price Quantity
63130120 µg$280
631302100 µg$750

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostE.coli
Target NameIL-1b, Catabolin, interleukin-1 beta, preinterleukin 1 beta, pro-interleukin-1-beta
SpeciesHuman
accession numberNP_000567.1
SourcesA DNA sequence encoding the mature form of human IL1β (NP_000567.1) (Ala 117-Ser 269) was expressed with a N-terminal Met.
Molecular WeightThe recombinant human IL1β consisting of 154 amino acids migrates with an apparent molecular mass of 17 kDa as estimated 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, Autoimmunity

Background Information

Human interleukin-1 beta (IL-1β) is a key proinflammatory cytokine that coordinates innate immune responses, including fever induction, leukocyte recruitment, and activation of endothelial and stromal cells. It is mainly produced by monocytes, macrophages, and dendritic cells following recognition of pathogens or tissue damage through pattern recognition receptors. IL-1β is synthesized as an inactive precursor, pro-IL-1β, and requires cleavage by caspase-1 within the inflammasome complex to generate its mature, biologically active form, making inflammasome activation a central control point in its regulation.

Structurally, IL-1β belongs to the IL-1 cytokine family and adopts a β-trefoil fold composed of a compact beta-sandwich-like architecture. It is a non-glycosylated, soluble protein that functions primarily as a monomer. IL-1β signals through the interleukin-1 receptor type I (IL-1R1), which forms a functional receptor complex with the IL-1 receptor accessory protein (IL-1RAcP). IL-1β is the principal ligand for this receptor system, and ligand binding initiates MyD88-dependent signaling cascades that activate NF-κB and MAPK pathways, driving expression of inflammatory genes.

Dysregulated IL-1β activity is strongly associated with inflammatory and autoimmune diseases such as rheumatoid arthritis, gout, inflammatory bowel disease, atherosclerosis, and autoinflammatory syndromes. Chronic overproduction contributes to sustained inflammation and tissue injury, whereas insufficient activation may impair host defense against infection. Therapeutically, IL-1β is targeted by biologics including monoclonal antibodies and receptor antagonists such as IL-1 receptor blockers. These therapies are used clinically to reduce excessive inflammation in autoinflammatory and rheumatologic conditions and are being explored in metabolic and cardiovascular diseases.

Data Sheets

Recombinant Human IL-1β 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.