Recombinant Human IL-29/IFN-lambda 1 Protein, CF

Recombinant Human IL‑29/IFN‑lambda 1 Protein (Catalog # 11240-IL) demonstrates anti-viral activity in HepG2 human hepatocellular carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 0.500-6.00 ng/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-29/IFN-lambda 1 Protein, CF Summary

• Additional Information: E. coli-expressed
• 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 0.500-6.00 ng/mL.
• Source: E. coli-derived human IL-29/IFN-lambda 1 protein
  Pro23-Thr200
• Accession #: Q8IU54.1
• N-terminal Sequence: Pro23
• 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: 20 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: 18-22 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 500 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 Human IL-29/IFN-lambda 1 Protein, CF

• cytokine Zcyto21
• IFNL1
• IFN-lambda 1
• IFN-lambda-1
• IL29
• IL-29
• interferon lambda-1
• interferon, lambda 1
• interleukin 29 (interferon, lambda 1)
• interleukin-29
• ZCYTO21

Background

IL-29, also known interferon-lambda 1 (IFN lambda 1), along with IL-28A (IFN lambda 2), IL-28B (IFN lambda 3) and IFN lambda 4, collectively comprise the type III subset of IFNs. IFN lambda s are class II cytokine receptor ligands distantly related to both members of the IL-10 family and to the type I IFN family (11-19% amino acid (aa) sequence identity). IL-29 is expressed only in humans and shares 67% and 69% aa sequence identity with human IL-28A and IL-28B, respectively. IFN lambda signaling was initially thought to be restricted to epithelial cells, but, recently, additional cell types have been shown to also respond. IFN lambda s have been shown to be induced by a variety of stimuli from influenza A and herpes viruses to lipopolysaccharides and double-stranded RNA. IL-29 signals through a unique receptor complex composed of IFN lambda R1 (IL-28RA) and the shared IL-10R2 chain, which is also a part of the receptor complexes for IL-10, IL-22, and IL-26. In humans, IL-29 is the most potent IFN lambda molecule, the most abundant IFN lambda molecule in serum, and the only IFN lambda molecule to display N-linked glycosylation. IL-29 is being investigated for its role in immunity, both innate and adaptive, as well as in autoimmune disorders. Additionally, the therapeutic potential of IL-29 in inflammatory diseases and its cancer fighting properties are being actively studied.

1. Vilcek, J. (2003) Nature Immunol. 4:8.
2. Sheppard, P. et al. (2003) Nature Immunol. 4:63.
3. Kotenko, S.V. et al. (2003) Nature Immunol. 4:69.
4. Gad, H.H. et al. (2009) J. Biol. Chem. (2009) 284:20869.
5. Miknis, Z.J. et al. (2010) J. Mol. Biol. 404:650.
6. Donnelly, R.P. et al. (2010) J. Interferon. Cytokine Res. 30:555.
7. Lazear, H.M. et al. (2015) Immunity. 43:15.
8. Ye, L. et al. (2019) Nat. Rev. Immunol. 19:614.
9. Goel, R.R. et al. (2021) Nat. Rev. Rheumatol. 17:349.
10. Kelm, N.E. et al. (2016) Crit. Rev. Oncol. Hematol. 106:91.
11. Wang, J.M. et al. (2019) J. Cell Mol. Med. 23:7926.

Bioinformatics

• Uniprot:
  • Q8IU54.1()