Recombinant Human IL-27 His-tag Biotinylated Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Chimera Protein (Catalog #
1479-TC) is immobilized at 0.500 μg/mL (100 μL/well), Biotinylated Recombinant Human IL‑27 His-tag (Catalog # BT2526) binds with an ED 50 of 4.00‑40.0 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived human IL-27 protein 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 | |
|
Accession # |
|
N-terminal Sequence |
Arg21 |
Structure / Form |
Biotinylated via amines |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
50 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
55-64 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, EDTA and CHAPS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-27 His-tag Biotinylated Protein, CF
Background
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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