17.3
#P18510
3557
Background
The founding members of the interleukin-1 (IL-1) superfamily include pro-inflammatory cytokines IL-1α and IL-1β, and a third protein that acts as an IL-1 receptor antagonist (IL-1RA). At least six similar proteins have been recently identified, including a homolog of IL-1RA (IL1F5). The three better-characterized proteins (IL-1a, IL-1b, and IL-1RA) are mainly expressed in macrophages, monocytes, and dendritic cells. IL-1a and IL-1b act as potent inflammatory cytokines that help regulate host defense and immune responses (1). Binding of these pro-inflammatory cytokines to an IL-1 receptor recruits adaptor proteins (such as IRAK) to the receptor. Phosphorylation of these adaptor proteins promotes downstream signaling cascades associated with the immune response (2). Altered expression of both IL-1a and IL-1b is associated with an extensive list of human disorders, including Alzheimer's disease, rheumatoid arthritis, psoriasis, and various forms of cancer (3,4). IL-1RA acts as an anti-inflammatory cytokine, binding the IL-1 receptor to limit the response to inflammation (5). Because it plays a key role in regulating the inflammatory response, recombinant IL-1RA is a therapeutic agent used in the treatment of diseases, such as rheumatoid arthritis. Alternatively, mutation of the corresponding IL-1RA gene may be associated with susceptibility to the development of specific cancers (6).
- Pelegrin, P. (2008) Drug News Perspect 21, 424-33.
- Ringwood, L. and Li, L. (2008) Cytokine 42, 1-7.
- Griffin, W.S. and Mrak, R.E. (2002) J Leukoc Biol 72, 233-8.
- Kamangar, F. et al. (2006) Cancer Epidemiol Biomarkers Prev 15, 1920-8.
- Arend, W.P. (2002) Cytokine Growth Factor Rev 13, 323-40.
- Sehouli, J. et al. (2002) Anticancer Res 22, 3421-4.
Endotoxin
Endotoxin levels are less than or equal to 1 EU / 1 μg hIL-1RA.
Purity
A greater than or equal to 95% purity was determined by SDS-PAGE.
Source / Purification
Recombinant human IL-1RA was expressed in E. coli and is supplied in a lyophilized form.
Bioactivity
The bioactivity of recombinant hIL-1RA was determined in an IL-1α induced D10.G4.1 cell proliferation assay. The ED50 of each lot is less than or equal to 50 ng/mL.
Background
The founding members of the interleukin-1 (IL-1) superfamily include pro-inflammatory cytokines IL-1α and IL-1β, and a third protein that acts as an IL-1 receptor antagonist (IL-1RA). At least six similar proteins have been recently identified, including a homolog of IL-1RA (IL1F5). The three better-characterized proteins (IL-1a, IL-1b, and IL-1RA) are mainly expressed in macrophages, monocytes, and dendritic cells. IL-1a and IL-1b act as potent inflammatory cytokines that help regulate host defense and immune responses (1). Binding of these pro-inflammatory cytokines to an IL-1 receptor recruits adaptor proteins (such as IRAK) to the receptor. Phosphorylation of these adaptor proteins promotes downstream signaling cascades associated with the immune response (2). Altered expression of both IL-1a and IL-1b is associated with an extensive list of human disorders, including Alzheimer's disease, rheumatoid arthritis, psoriasis, and various forms of cancer (3,4). IL-1RA acts as an anti-inflammatory cytokine, binding the IL-1 receptor to limit the response to inflammation (5). Because it plays a key role in regulating the inflammatory response, recombinant IL-1RA is a therapeutic agent used in the treatment of diseases, such as rheumatoid arthritis. Alternatively, mutation of the corresponding IL-1RA gene may be associated with susceptibility to the development of specific cancers (6).
Background References
Cross-Reactivity Key
H: human M: mouse R: rat Hm: hamster Mk: monkey Vir: virus Mi: mink C: chicken Dm: D. melanogaster X: Xenopus Z: zebrafish B: bovine Dg: dog Pg: pig Sc: S. cerevisiae Ce: C. elegans Hr: horse GP: Guinea Pig Rab: rabbit All: all species expected
Trademarks and Patents
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