Detects mouse IL‑28A/IFN‑ lambda 2 in direct ELISAs and Western blots. In Western blots, approximately 50% cross-reactivity with recombinant mouse IL‑28B is observed and less than 5% cross-reactivity with recombinant human (rh) IL-28A and rhIL-28B is observed.
Measured by its ability to neutralize IL‑28A/IFN‑ lambda 2 inhibition of EMCV-induced cytopathy in the HepG2 human hepatocellular carcinoma cell line. Sheppard, P. et al. (2003) Nat. Immunol. 4:63. The Neutralization Dose (ND50) is typically 3-15 µg/mL in the presence of 20 ng/mL Recombinant Mouse IL‑28A/IFN‑ lambda 2.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
IL‑28A/IFN‑ lambda 2 Inhibition of EMCV-induced Cytopathy and Neutralization by Mouse IL‑28A/IFN‑ lambda 2 Antibody.
Recombinant Mouse IL‑28A (Catalog # 4635‑ML) reduces the Encephalomyocarditis Virus (EMCV)-induced cytopathy in the HepG2 human hepatocellular carcinoma cell line in a dose-dependent manner (orange line). Inhibition of EMCV activity elicited by Recombinant Mouse IL‑28A (20 ng/mL) is neutralized (green line) by increasing concentrations of Sheep Anti‑Mouse IL‑28A Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF4635). The ND50 is typically 3‑15 µg/mL.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-28A/IFN-lambda 2
IL-28A (also named interferon-lambda 2, IFN-lambda 2), IL-28B (IFN-lambda 3) and IL-29 (IFN-lambda 1) are type III interferons that are class II cytokine receptor ligands (1‑4). They are distantly related to members of the IL-10 family and type I IFN family (1‑4). Mouse IL-28A cDNA encodes a 193 amino acid (aa) protein with a 19 aa signal peptide and a 174 aa mature protein that lacks N-glycosylation sites. Mature mouse IL-28A shares 81% and 66% aa sequence identity with rat and human IL-28A, respectively, and functions across species (5). Mouse IL-28A and IL-28B share 97% aa identity; the mouse lacks a functional IL-29 gene (4). Type III interferons are widely expressed, but are mainly produced by antigen presenting cells in response to viruses and double-stranded RNA that interact with Toll-like receptors or RIG-1 family helicases (2‑6). They signal through a widely expressed receptor that is a heterodimer of the IL-10 receptor beta (IL-10 R beta ) and IL-28 receptor alpha (IL-28 R alpha ; also called IFN-lambda R1) (2, 3, 7, 9). Interaction of either type I or type III IFNs with their receptors activates similar pathways, including JAK tyrosine kinase activation, STAT phosphorylation and formation of the IFN-stimulated regulatory factor 3 (ISGF-3) transcription factor complex (1‑3). Both type I and III IFNs induce antiviral activity and upregulate MHC class I antigen expression (2‑6). Cell lines responsive to type III IFNs are also responsive to type I IFNs, but in general, higher concentrations of type III IFNs are needed for similar in vitro responses (8). In vivo, however, type III IFNs enhance levels of IFN-gamma in serum, suggesting that the robust antiviral activity of type III IFNs may stem in part from activation of the immune system (5, 7). Anti-proliferative and antitumor activity in vivo has also been shown for type III IFNs (9‑11).
Chen, Q. et al. (2006) Vitam. Horm. 74:207.
Sheppard, P. et al. (2003) Nat. Immunol. 4:63.
Kotenko, S.V. et al. (2003) Nat. Immunol. 4:69.
Bartlett, N.W. et al. (2005) J. Gen. Virol. 86:1589.
Ank, N. et al. (2006) J. Virol. 80:4501.
Onoguchi, K. et al. (2007) J. Biol. Chem. 282:7576.
Siebler, J. et al. (2007) Gastroenterology 132:358.
Meager, A. et al. (2005) Cytokine 31:109.
Lasfar, A. et al. (2006) Cancer Res. 66:4468.
Sato, A. et al. (2006) J. Immunol. 176:7686.
Zitzmann, K. et al. (2006) Biochem. Biophys. Res. Commun. 344:1334.
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