Recombinant Human Interleukin-1 beta (IL1B) (Active)

Interleukin-1 beta; IL-1 beta; Catabolin; IL1B; IL1F2

Recombinant Human IL1B protein (Active)

IL1B

P01584

117-269aa

Homo sapiens (Human)

APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS

N-terminal 10xHis-tagged

Active Protein & In Stock Protein

Mammalian cell

Immunology

Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection. Miscellaneous The IL1B production occurs in 2 steps, each being controlled by different stimuli. First, inflammatory signals, such as LPS, stimulate the synthesis and promote the accumulation of cytosolic stores of pro-IL1B (priming) . Then additional signals are required for inflammasome assembly, leading to CASP1 activation, pro-IL1B processing and eventually secretion of the active cytokine. IL1B processing and secretion are temporarily associated. Activity regulation (Microbial infection) Cleavage by S.pyogenes cysteine protease SpeB promotes its activation independently of CASP1. SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota.

Less than 1.0 EU/μg as determined by LAL method.

Greater than 90% as determined by SDS-PAGE.

Yes

Measured by its binding ability in a functional ELISA.Immobilized Human IL1B at 5 μg/mL can bind Human IL1R2 (CSB-MP011622HU1) . The EC50 is 89.65-100.5 ng/mL.

Lyophilized powder

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

21.0 kDa

Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Wilson R.K. Nature 434:724-731 (2005)

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.