Recombinant Human IL-27 His-tag Biotinylated Protein, CF

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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 ...read more
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, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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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 ED50 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-terminusC-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
  • Bioactivity
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

  • IL-27 p28 subunit
  • IL-27 subunit alpha
  • IL27
  • IL-27
  • IL27A
  • IL-27-A
  • IL27-A
  • IL27p28
  • IL30
  • interleukin 27
  • interleukin 30
  • interleukin-27 subunit alpha
  • MGC71873
  • p28IL-27A

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).
  1. Boulay, J-L. et al. (2003) Immunity 19:159.
  2. Trinchieri, G. et al. (2003) Immunity 19:641.
  3. Murakami, M. et al. (2004) Growth Factors 22:75.
  4. Cordoba-Rodriguez, R. and D.M. Frucht (2003) Exp. Opin. Biol. Ther. 3:715.
  5. Devergne, O. et al. (1996) J. Virology 70:1143.
  6. Pflanz, S. et al. (2002) Immunity 16:779.
  7. Villarino, A.V. et al. (2004) J. Immunol. 173:715.
  8. Pflanz, S. et al. (2004) J. Immunol. 172:2225.
  9. Scheller, J. et al. (2005) Biochem. Biophys. Res. Commun. 326:724.
  10. Holscher, C. (2004) Med. Microbiol. Immunol. (Berl).193:1.

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