Recombinant Human IL-27 His-tag Biotinylated Protein, CF
Recombinant Human IL-27 His-tag Biotinylated Protein, CF Summary
Product Specifications
| Human IL-27 EBI-3 (Arg21-Lys229) Accession # Q14213.2 | Human IL-27 p28 (Phe29-Pro243) Accession # AAM34498.1 | 6-His tag |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
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.
BT2526
| Formulation | Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, EDTA and CHAPS with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile water. |
| 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.
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Scientific Data
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Measured by its binding ability in a functional ELISA. When Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Chimera Protein (1479-TC) is immobilized at 0.500 μg/mL (100 μL/well), Recombinant Human IL‑27 His-tag Biotinylated Protein (Catalog # BT2526) binds with an ED50 of 4.00‑40.0 ng/mL.
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2 μg/lane of Recombinant Human IL-27 His-tag Biotinylated Protein (Catalog # BT2526) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-64 kDa.
Reconstitution Calculator
Background: IL-27
IL-27 is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines (1). It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the 28 kDa glycoprotein that is related to the p35 chain of IL-12 (2-4). The human EBI3 gene encodes a 229 amino acid (aa) precursor that contains a 20 aa signal peptide and 209 aa mature protein (5). The mature region contains two potential N-linked glycosylation sites, two fibronectin type III domains, and two pairs of conserved cysteine residues with a WSXWS-like motif that places the molecule in the hematopoietin receptor family (5). Although p40, the EBI3 counterpart in IL-12, is known to form homodimers, there is no evidence to date that EBI3 also homodimerizes. Human EBI3 is 61% aa identical to mouse EBI3. The human p28 gene encodes a 243 aa precursor that contains a 28 aa signal sequence and 215 aa mature region (6). The mature region is characterized by the presence of four alpha-helices, placing it in the IL-6 family of helical cytokines. Human p28 is 74% aa identical to mouse p28. IL-27 is expressed by monocytes, endothelial cells and dendritic cells (7). IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX-1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1 (6, 8, 9). IL-27 has both anti- and proinflammatory properties. As an anti-inflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity (3, 7). At the onset of infection, IL-27 induces an IL-12 receptor on naïve CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development) (10).
- Boulay, J-L. et al. (2003) Immunity 19:159.
- Trinchieri, G. et al. (2003) Immunity 19:641.
- Murakami, M. et al. (2004) Growth Factors 22:75.
- Cordoba-Rodriguez, R. and D.M. Frucht (2003) Exp. Opin. Biol. Ther. 3:715.
- Devergne, O. et al. (1996) J. Virology 70:1143.
- Pflanz, S. et al. (2002) Immunity 16:779.
- Villarino, A.V. et al. (2004) J. Immunol. 173:715.
- Pflanz, S. et al. (2004) J. Immunol. 172:2225.
- Scheller, J. et al. (2005) Biochem. Biophys. Res. Commun. 326:724.
- Holscher, C. (2004) Med. Microbiol. Immunol. (Berl).193:1.
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