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Human IL-1 beta Recombinant Protein
- Catalog Number:
- RP0877H
- Availability:
- In stock
- Application:
- Cell Culture, ELISA Standard, ELISpot Control, Western Blot Control
- 100% Homology:
- Homo sapiens (human), Pan paniscus (pygmy chimpanzee), Pan troglodytes (chimpanzee)
- Human IL-1β (catalog RP0877H) is a yeast-derived cytokine supplied lyophilized without carrier protein in 10% trehalose; it has no affinity tags and is naturally endotoxin-free, and should be reconstituted in sterile PBS that contains at least 0.1% carrier protein. The protein is ~17.4 kDa, 153 amino acids long (full sequence provided), and >98% pure by SDS-PAGE, with 100% amino-acid homology to human, chimpanzee, and bonobo. Store at -20°C (stable up to twelve months from date of receipt; working aliquots with carrier protein stable ~3 months) and avoid repeated freeze/thaw cycles. Product origin is the USA. It is commonly used to study IL-1 signaling and inflammatory responses (including activation of immune cells and cytokine production); typical experimental uses include cell-culture stimulation and dosing studies, cytokine signaling assays, ELISA and neutralization assays, flow-cytometry and Western blot controls, and antibody generation/validation. Kingfisher Biotech products are supplied for research applications and are not intended for medicinal, diagnostic, or therapeutic use.
| Amino Acid Sequence | APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS (153) |
| Endotoxin | Naturally endotoxin-free |
| Storage Conditions | -20°C |
| Molecular Weight | 17.4 kDa |
| Purity | >98% as visualized by SDS-PAGE analysis. |
| Country Of Origin | USA |
- Human Interleukin-1 Beta (IL-1β) is a potent pro-inflammatory cytokine produced primarily by activated macrophages, monocytes, and dendritic cells in response to infection, tissue injury, or danger-associated molecular patterns. Synthesized as an inactive precursor (pro-IL-1β), it is cleaved into its active form by caspase-1 within multiprotein inflammasome complexes-most notably the NLRP3 inflammasome-and subsequently signals through the IL-1 receptor type 1 (IL-1R1), activating NF-κB and MAPK pathways that drive fever, leukocyte recruitment, endothelial activation, and acute-phase protein production. IL-1β plays a central role in host defense against bacterial, viral, and fungal pathogens, but dysregulated or excessive IL-1β signaling contributes to a wide range of inflammatory and autoimmune conditions, including rheumatoid arthritis, gout, inflammatory bowel disease, type 2 diabetes, atherosclerosis, sepsis, and cytokine release syndromes. Elevated IL-1β is also implicated in neuroinflammatory disorders and certain cancers, where it can promote tumor progression and immune modulation. As both a biomarker and therapeutic target, IL-1β has been the focus of targeted biologic therapies such as IL-1 receptor antagonists and anti-IL-1β monoclonal antibodies. Consequently, human IL-1β is central to research on inflammasome biology, chronic inflammation, metabolic disease, and development of precision anti-inflammatory treatments.
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