Measured by its ability to inhibit IL-1 alpha -dependent proliferation in D10.G4.1 mouse helper T cells. Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272. The ED50 for this effect is 0.02-0.06 µg/mL in the presence of 50 pg/mL of recombinant porcine IL-1 alpha .
Source
E. coli-derived porcine IL-1ra/IL-1F3 protein His26-Gln177, with an N-terminal Met
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
17 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publication using 780-RA in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in NaH2PO4 and NaCl with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Porcine IL-1ra/IL-1F3 Protein
DIRA
ICIL-1ra
IL1F3
IL-1F3
IL1ra
IL-1ra
IL-1ra3
IL1RN
IL-1RN
interleukin 1 receptor antagonist
IRAP
MVCD4
Background
IL-1ra was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The naturally-occurring, fully glycosylated form has an apparent molecular weight of about 25,000 Daltons. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha . It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptors (I and II) on human cells, but reportedly will not block binding to the type II receptor on murine pre-B cell lines. The recombinant, non-glycosylated form of IL-ra blocks binding of IL-1 to its receptor equally as well as the naturally-occurring, glycosylated form. The IL-1ra has been shown to block the inflammatory responses induced by IL-1 both in vitro and in vivo. Human, mouse and rat IL-1ra all share approximately 80% homology with porcine IL-1ra.
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