Egyptian Rousette Bat IL-1 beta Recombinant Protein

Catalog Number:
RP2120BT
Application:
Cell Culture, Control, ELISA, ELISpot Control, Western Blot Control
100% Homology:
Rousettus aegyptiacus (Egyptian rousette)
  • Bat IL-1β (Interleukin-1 beta) (catalog RP2120BT) is a yeast-derived cytokine supplied lyophilized without carrier protein in 10% trehalose; it contains no affinity tags, is naturally endotoxin-free, and should be reconstituted in sterile PBS with at least 0.1% carrier protein. The protein is ~18.4 kDa, 161 amino acids in length (full sequence provided), and >98% pure by SDS-PAGE, with 100% amino-acid homology to Egyptian rousette bat. It is stable for up to twelve months at -20 °C from receipt, with working aliquots (with carrier protein) stable for ~3 months; avoid repeated freeze/thaw cycles. The product is manufactured in the USA. It is commonly used to study IL-1 signaling and inflammatory responses, including regulation of immune activation, cytokine production, and innate immune pathways; typical applications include cell-based assays, cytokine signaling studies, inflammation research, ELISA and neutralization assays, flow cytometry and Western blot controls, and antibody development or validation. Kingfisher Biotech products are supplied for research applications only and are not intended for medicinal, diagnostic, or therapeutic use.
Amino Acid SequenceSCTHDDGYVC DAPLRSLSFR LRDINQKSLV LSGPHELQAL HLNRQDASRQ VVFCMSFMPE ENGDKIPVAL GIKENNLYLS CVMKDGKPSL QLETVYLEDQ SKMDRRFVFN KTEIKGKVEF ESALYPSWYI STSQMEQMPV FLGSSRGGQD ITDFTMEVLS R (161)
EndotoxinNaturally endotoxin-free
FormLyophilized
Storage Conditions-20°C
Molecular Weight18.4kDa
Purity>98% as visualized by SDS-PAGE analysis.
Affinity TagNone
aminoAcids161
Carrier ProteinNone
Expression SystemYeast
FormLyophilized
Country Of OriginUSA
Egyptian Rousette Bat (Rousettus aegyptiacus) Interleukin-1 Beta (IL-1β) is a potent pro-inflammatory cytokine produced primarily by activated macrophages and other innate immune cells following inflammasome activation in response to infection or tissue injury. Like in other mammals, IL-1β is synthesized as an inactive precursor (pro–IL-1β) and requires cleavage by caspase-1 within the inflammasome complex to become biologically active, after which it signals through the IL-1 receptor (IL-1R1) to activate NF-κB and MAPK pathways that drive fever, leukocyte recruitment, and amplification of inflammatory responses. In R. aegyptiacus, a natural reservoir host for filoviruses such as Marburg virus, IL-1β is of particular interest because bats are capable of controlling viral replication while exhibiting limited clinical inflammation, suggesting tightly regulated inflammasome and IL-1β signaling. Characterization of IL-1β responses in Egyptian Rousette bats supports studies of innate immune activation, viral tolerance, and mechanisms that prevent excessive immunopathology during infection. Understanding IL-1β dynamics in this species enhances its value as a reservoir host model for emerging zoonotic viruses and provides comparative insight into inflammatory regulation and host–pathogen interactions relevant to human infectious disease research.
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