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. 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. 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. 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. 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.
Product Properties
Synonyms |
IL-1RN, IRAP |
Accession |
O18999 |
GeneID |
100034236 |
Source |
E.coli-derived Equine IL-1RA, His26-Gln177. |
Molecular Weight |
Approximately 17.4 kDa. |
AA Sequence |
HPLGKRPCKM QAFRIWDVNQ KTFYMRNNQL VAGYLQESNT KLQEKIDVVP IEPDALFLGL HGRKLCLACV KSGDEIRFQL EAVNITDLSK NKEENKRFTF IRSNSGPTTS FESAACPGWF LCTAQEADRP VSLTNKPKES FMVTKFYLQE DQ |
Tag |
None |
Physical Appearance |
Sterile Filtered White lyophilized (freeze-dried) powder. |
Purity |
> 95% by SDS-PAGE and HPLC analyses. |
Biological Activity |
The ED50 as determined by inhibiting IL-1α-dependent proliferation of murine D10S cells is less than 3.0 μg/mL, corresponding to a specific activity of > 333 IU/mg in the presence of 50 pg/mL rHuIL-1α. Fully biologically active when compared to standard. |
Endotoxin |
< 1.0 EU per 1μg of the protein by the LAL method. |
Formulation |
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. |
Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
Shipping and Storage
The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year.
Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.
Cautions
1. Avoid repeated freeze-thaw cycles.
2. For your safety and health, please wear lab coats and disposable gloves for operation.
3. For research use only!
HB220425