Recombinant Cynomolgus Monkey IL-27 His-tag Protein, CF Summary
Details of Functionality |
Measured in an anti-viral assay using HepG2 human hepatocellular carcinoma cells infected with encephalomyocarditis (EMC) virus. Sheppard, P. et al. (2003) Nat. Immunol. 4:63. The ED50 for this effect is 0.75-6.0 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey IL-27 protein Cynomolgus Monkey EBI-3 (Arg36-Lys244) Accession # XP_005587614.1 | GSGSSRGGSGSGGSGGGGSKL | Cynomolgus Monkey IL-27a
*Unique sequence | 6-His tag | N-terminus | | | C-terminus | |
* Unique Sequence: This gene was isolated from a cynomolgus monkey cDNA library. The closest match to the obtained sequence is a genomic prediction for rhesus monkey, Accession XP_028697194.1 (Phe42-Pro254, A170T). |
Accession # |
|
N-terminal Sequence |
Arg36 |
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 |
54-65 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 PBS 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 PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Monkey IL-27 His-tag 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 50 kDa glycoprotein that is related to the p40 subunit of IL-12 and
IL-23, and p28, a 28 kDa glycoprotein that is related to the p35 chain of IL-12
(2-4). The Cynomolgous EBI3 gene encodes a 244 amino acid (aa) precursor that
contains a 36 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. Cynomolgous monkey EBI3 is
94% aa identical to Human EBI3. The Cynomolgous monkey p28 gene encodes a 254 aa precursor
that contains a 41 aa signal sequence and 214 aa mature regions. The mature
region is characterized by the presence of four alpha -helices, placing it in
the IL-6 family of helical cytokines. Cynomolgous monkey p28 is 92% aa identical to human
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 (6, 8, 9). IL-27 has both anti- and
proinflammatory properties. As an anti-inflammatory cytokine, 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. 193:1.
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