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Interleukin-1 (IL-1) Receptor Antagonist, human
| Full Name |
Interleukin-1 (IL-1) Receptor Antagonist, Human
|
Abbreviated Name-1 |
rHuIL-1ra; IL1 Receptor Antagonist; Interleukin-1 Receptor Antagonist; Interleukin1 Receptor Antagonist |
| Documents |
Document-MSDS: 13682_20110412044642.PDF (PDF) |
| Figures |
| Reference |
|---|
Dayer JM, et al. Adipose Tissue Has Anti-Inflammatory Properties: Focus on IL-1 Receptor Antagonist (IL-1Ra). Ann. N. Y. Acad. Sci. Jun 2006; 1069: 444-453.
Bessler H, et al. Postoperative pain, morphine consumption, and genetic polymorphism of IL-1beta and IL-1 receptor antagonist. Neurosci. Lett. Aug 2006; 404(1-2): 154-158.
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Description |
Interleukin-1 receptor antagonist (IL-1ra) is a member of the IL-1 family. Endogenous IL-1ra is produced in numerous animal disease models as well as in human autoimmune and chronic inflammatory diseases. It binds to IL-1 receptors in competition with IL-1, but does not elicit intracellular response from this binding. Its role in counteracting the proinflammatory effects of IL-1 is being studied by numerous research groups. IL-4 and IL-13 have been shown to amplify the stimulatory effect of IL1-beta on the production of soluble and intracellular forms of IL1-ra. The regulated expression of IL1ra in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts the synthesis of IL-1ra is markedly enhanced by IL-1 , TNF-alpha , or PDGF. Recombinant Human IL-1RN produced in E. coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17,258 Da. |
Source |
E. coli |
M.W. |
17,258 Da |
Purity |
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel. |
Endotoxin Level |
Less than 0.1 ng/µg (IEU/µg) of IL-1 ra. |
Specific Activity |
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml, corresponding to a Specific Activity of 2.0×106 IU/mg. |
Storage |
Lyophilized rHuIL-1 ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rHuIL-1ra should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid repeated freeze-thaw cycles. |
Formulation |
The protein was lyophilized after extensive dialysis against 50mM Tris-HCl, pH7.5, 200mM NaCl buffer. |
Reconstitution |
It is recommended to reconstitute the lyophilized rHuIL-1ra in sterile 18 MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. |
Quantitation |
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Sequence analysis |
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly. |
Note |
; |
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