IL1RN
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
> 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.
Active
analysis The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly. p to grams level.
Attributs du produit
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 aof 2.0×106 IU/mg
Pureté
> 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.
IL1RN
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
IL1RN
Origine: Humain
Hôte: HEK-293T Cells
Recombinant
> 95 % as analyzed by SDS-PAGE and HPLC.
Active
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
It is recommended to reconstitute the lyophilized rHuIL-1ra in sterile 18 M-omega-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. Quantitation
Stock
-20 °C
Hedl, Abraham: "Distinct roles for Nod2 protein and autocrine interleukin-1beta in muramyl dipeptide-induced mitogen-activated protein kinase activation and cytokine secretion in human macrophages." dans: The Journal of biological chemistry, Vol. 286, Issue 30, pp. 26440-9, (2011) (PubMed).
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. Synonym: rHuIL-1ra, IL1 Receptor Antagonist, Interleukin-1 Receptor Antagonist, Interleukin1 Receptor Antagonis. Formulation: The protein was lyophilized after extensive dialysis against 50mM Tris-HCl, pH7.5, 200mM NaCl buffer.