Human Interleukin 1 beta Recombinant

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Human Interleukin 1 beta Recombinant

$70.00$3,500.00


accession P01584


Source Optimized DNA sequence encoding Human Interleukin-1 betamature chain was expressed in Escherichia Coli.
Molecular weight Mature Human IL-1 beta, is generated by the proteolytic removal of the signal peptide and propeptide.The molecule has a calculated molecular mass of approximately17 kDa. Recombinant IL-1 betais a disulfide-linked monomer protein consisting of two amino acid residue subunits. Recombinant IL-1 beta migrates as an approximately17 kDa protein under non-reducing and reducing conditions in SDS-PAGE.
Purity >97%, as determined by SDS-PAGE and HPLC
Biological Activity The ED(50) as determined by thedose-dependent proliferation of murine D10S cells, was found to be ≤.0 pg/ml, corresponding to a specific activity of ≥2 x units/mg.
Protein Sequence MAEVPELASE MMAYYSGNED DLFFEADGPK QMKCSFQDLD LCPLDGGIQL RISDHHYSKG FRQAASVVVA MDKLRKMLVP CPQTFQENDL STFFPFIFEE EPIFFDTWDN EAYVHDAPVR SLNCTLRDSQ QKSLVMSGPY ELKALHLQGQ DMEQQVVFSM SFVQGEESND KIPVALGLKE KNLYLSCVLK DDKPTLQLES VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST SQAENMPVFL GGTKGGQDIT DFTMQFVSS
Endotoxin Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than.1 ng/µg(1EU/µg).
Presentation IL-1 beta was lyophilized from a.2 μm filtered PBS pH.0.
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least years from date of receipt at -20° C. Upon reconstitution, this cytokine can be stored in working aliquots at° -° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.


Interactor P29466
Biological Process Inflammatory-response
Molecular function Cytokine
Molecular function Mitogen
Molecular function Pyrogen

Methods

Migration assays

  • HUVECs were seeded at 15–20×103/well and cultured to 90% confluence on 24-well transwell tissue culture inserts (24-well plate with inserts, 5 µm pore/6.5 mm, TC-treated) as previously described 3 receptor agonists and antagonists were present during the migration in both transwell compartments.
  • Migration experiments displayed an inter-donor variability in the absolute number of migrating T cells, thus for each experiment migration data have been normalized considering the number of counted cells in control conditions as 100%.

Islet isolation, culture, and exposure to different beta-cell inhibitory substances

  • Following the initial culture period, islets were cultured for an additional 6–24 hours in CMRL 1066 containing antibiotics, 2 mM glutamine and one of the following supplements: 0.5 mM sodium palmitate solubilized in 0.5% (weight/volume) fatty acid and lipopolysaccaride free bovine serum albumin (BSA) ; recombinant human Interleukin 1beta (IL-1ß (50 units/ml) and Interferon-gamma (IFN-γ) (1,000 units/ml) ; 100 mM hydrogen peroxide; 2 mM DETA/NO or 10 mM streptozotocin (STZ) .
  • To some of the groups 10 µM of Imatinib was added at different time points prior to the addition of test substances given above.
  • To controls equal amounts of vehicle (DMSO) were supplemented.

The placenta releases sST2.

100 ng/ml IL-1β
  • C) Placental explants release sST2, secretion was increased by treatment with TNFα and IL-1β (100 ng/ml) and hypoxia-reperfusion injury, and was decreased under hypoxic conditions (n = 3).

Effect of CORM-2 on HO-1 protein (A) and mRNA expression (B) in OA synoviocytes.

IL-1β
  • Cells were stimulated with IL-1β (10 ng/ml) for 24 h and 16 h in the presence or absence of CORM-2 (50, 100, 200 µM) or RuCl3 (200 µM).

Functional characterization of mutant N1.

IL-1β
  • Cells were treated with IL-1β, lysed and the relative fold activation of NF-κB activity was determined.