Recombinant Equine IL-1ra/IL-1F3 Protein Summary
Product Specifications
His26-Gln177, with an N-terminal Met
Analysis
Product Datasheets
2466-RA (with carrier)
2466-RA/CF (carrier free)
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
2466-RA
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and DTT with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
2466-RA/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and DTT. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: IL-1ra/IL-1F3
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).
- Arend, W.P. et al. (1998) Annu. Rev. Immunol. 16:27.
- Roux-Lombard, P. (1998) Eur. Cytokine Netw. 9:565.
- 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.
Citation for Recombinant Equine IL-1ra/IL-1F3 Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
-
Proteomic analysis of tendon extracellular matrix reveals disease stage-specific fragmentation and differential cleavage of COMP (cartilage oligomeric matrix protein).
Authors: Dakin S, Smith R, Heinegard D, Onnerfjord P, Khabut A, Dudhia J
J Biol Chem, 2014-01-07;289(0):4919.
Species: Equine
Sample Types: Whole Tissue
Applications: Bioassay
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Equine IL-1ra/IL-1F3 Protein
There are currently no reviews for this product. Be the first to review Recombinant Equine IL-1ra/IL-1F3 Protein and earn rewards!
Have you used Recombinant Equine IL-1ra/IL-1F3 Protein?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
