Equine IL-1ra/IL-1F3 Biotinylated Antibody
Equine IL-1ra/IL-1F3 Biotinylated Antibody Summary
Accession # O18999.1
Equine IL-1ra/IL-1F3 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Secreted equine IL-1 receptor antagonist (IL-1ra) is a presumably 22 - 25 kDa glycoprotein produced by variety of cell types that antagonizes IL-1 activity (1 - 3). It is a member of the IL-1 family of proteins that includes IL-1 alpha and IL-1 beta. Although there is little amino acid (aa) identity (< 30%) among the three IL-1 family members, all molecules bind to the same receptors, all show a beta -trefoil structure, and all are believed to have evolved from a common ancestral gene (1 - 4). Equine IL-1ra is synthesized as a 177 aa precursor that contains a 25 aa signal sequence plus a 152 aa mature region. There is one intrachain disulfide bond and one potential N-linked glycosylation site (3, 5, 6). Mature equine sIL-1ra is 78%, 78%, 80%, 82%, and 76% aa identical to mature mouse, human, porcine, canine and bovine IL-1ra, respectively. In human, three non-secreted IL-1ra isoforms have also been identified. It is unknown if such an analogous situation exists in equine. Cells known to secrete IL-1ra include fibroblasts, vascular smooth muscle cells, intestinal columnar epithelium, chondrocytes, macrophages, mast cells, neutrophils and hepatocytes.
There are two type I transmembrane glycoprotein receptors for IL-1ra. The first is the bioactive 80 kDa type I IL-1 receptor (IL-1 RI), and the second is the inert (decoy) 65 kDa type II IL-1 receptor. IL-1ra binding to IL-1 RI competitively blocks IL-1 ( alpha or beta ) binding to the same receptor. This results in receptor ligation without activation (1, 7). The type II IL-1 receptor is inert, and any binding of IL-1ra not only fails to block co-existing IL-1 activity, but may actually potentiate it by removing an IL-1 antagonist. Functionally, all activities attributed to IL-1ra are explained by its role as a competitive inhibitor of IL-1 binding to IL-1 RI (1, 2, 8, 9).
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- Dayer-J-M. (2002) Clin. Exp. Rheumatol. 20(27):S14.
- Eisenberg, S.P. et al. (1991) Proc. Natl. Acad. Sci. USA 88:5232.
- Kato, H. et al. (1997) Vet. Immunol. Immunopathol. 56:221.
- Howard, R.D. et al. (1998) Am. J. Vet. Res. 59:712.
- Dinarello, C.A. (1997) Semin. Oncol. (Suppl 9):S9.
- Irikura, V.M. et al. (2002) J. Immunol. 169:393.
- Arend, W.P. and C. Gabay (2000) Arth. Res. 2:245.
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