assay
≥97% (SDS-PAGE)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
impurities
≤1.0 EU/μg Endotoxin (EU/μg IL-1α)
shipped in
ambient
storage temp.
−70°C
Quality Level
Biochem/physiol Actions
ED₅₀ = 3-7 pg/ml as measured in a cell proliferation assay.
Disclaimer
Toxicity: Standard Handling (A)
General description
Recombinant, human interleukin-1α expressed in E. coli. A 159 amino acid polypeptide derived from mature IL-1α. Synthesized in vivo as a 271 amino acid residue (31 kDa) precursor that is subsequently cleaved into the mature polypeptide. Shows ~25% amino acid sequence identity with IL-1β, a distinct gene product sharing the same cell surface receptors as IL-1α. Produced by activated macrophages and many other cell types, the IL-1 proteins mediate a variety of effects on the differentiation and function of many cell types involved in inflammatory and immune responses. Potent stimulator of bone resorption and stimulator of nuclear phospholipase C. Induces nitric oxide synthase. Effects include stimulation of T-cell, B-cell, neutrophil, and fibroblast proliferation; induction of prostaglandin, leukotriene, and acute-phase hepatic protein synthesis; induction of proteinases in synovial fibroblasts and articular chondrocytes. IL-1 is also known to induce fever, slow-wave sleep, and bone resorption. 1 µg is equivalent to 1.6 x 105 WHO units.
Other Notes
Tsan, M.F., and White, J.E. 1994. Am. J. Physiol. 266, L316.
Kilbourn, R.G., et al. 1992. J. Natl. Cancer Inst. 84, 1008.
Dinarello, C.A., et al. 1991. Blood77, 1627.
Casagli, M.C., et al. 1989. Biochem. Biophys. Res. Commun.162, 357.
Symons, J.A., et al. 1987. In Lymphokines and Interferons, A Practical Approach (Clemens, M.J., et al. Eds.) Oxford IRL Press, p. 272.
March, C.J., et al. 1985. Nature315, 641.
Kampschmidt, R.F. 1984. J. Leuk. Biol.36, 341.
Kilbourn, R.G., et al. 1992. J. Natl. Cancer Inst. 84, 1008.
Dinarello, C.A., et al. 1991. Blood77, 1627.
Casagli, M.C., et al. 1989. Biochem. Biophys. Res. Commun.162, 357.
Symons, J.A., et al. 1987. In Lymphokines and Interferons, A Practical Approach (Clemens, M.J., et al. Eds.) Oxford IRL Press, p. 272.
March, C.J., et al. 1985. Nature315, 641.
Kampschmidt, R.F. 1984. J. Leuk. Biol.36, 341.
Physical form
Lyophilized from sterile-filtered 20 mM Tris-HCl, 50 µg BSA/µg IL-1α, pH 8.3.
Preparation Note
Following reconstitution, aliquot and freeze (-70°C) for long term storage or refrigerate (4°C) for short term storage. Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 1 month at 4°C or for up to 3 months at -70°C.
Reconstitute with sterile PBS containing ≥0.1% HSA or BSA.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
C J March et al.
Nature, 315(6021), 641-647 (1985-06-20)
Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-1 alpha and IL-1 beta), were isolated from a macrophage cDNA library. The primary translation products of the genes are 271 and 269 amino acids
Interleukin-1alpha induced protection against pulmonary oxygen toxicity.
M F Tsan et al.
The American journal of physiology, 266(3 Pt 1), L316-L317 (1994-03-01)
R G Kilbourn et al.
Journal of the National Cancer Institute, 84(13), 1008-1016 (1992-07-01)
Interleukin-1-alpha (IL-1) is a cytokine with potentially therapeutic immunoproliferative and tumoricidal activities. Preliminary clinical studies suggest that use of IL-1 may be restricted by dose-limiting hypotension. The purpose of this study was to investigate the role of nitric oxide (NO.)
C A Dinarello
Blood, 77(8), 1627-1652 (1991-04-15)
The polypeptide cytokine interleukin-1 (IL-1) affects nearly every tissue and organ system. IL-1 is the prototype of the pro-inflammatory cytokines in that it induces the expression of a variety of genes and the synthesis of several proteins that, in turn
M C Casagli et al.
Biochemical and biophysical research communications, 162(1), 357-363 (1989-07-14)
Human recombinant interleukin 1 beta produced in Escherichia coli and in Saccharomyces cerevisiae was purified to homogeneity by a combination of ion exchange, gel filtration and hydroxylapatite column chromatography. The two proteins, both expressed in the mature form, differ in
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