Cell Signaling Technology

Product Pathways - Jak/Stat Pathway

IFN-α (8C21) Mouse mAb #3115

Applications Reactivity MW (kDa) Source Isotype
W IP H 19 Mouse IgG1 and kappa light chain

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

IFN-α (8C21) Mouse mAb detects human interferon-alpha proteins at various concentrations. This antibody does not cross-react with human interferon-β and -γ.

Source / Purification

Monoclonal antibodies are produced by immunizing mice with purified natural human interferon-α proteins.

Western Blotting

Western Blotting

Western blot analysis of natural human interferon-α proteins at various concentrations, using IFN-α (8C21) Mouse mAb.

Background

Interferons (IFNs) appear both locally and systematically early after viral infection and participate in limiting the spread of infection. They also affect cell differentiation, growth, surface antigen expression and immunoregulation (1). There are three naturally occurring interferons: α, β and γ. IFN-α is derived from lymphoblastic tissue and has a number of therapeutic applications in the treatment of various human cancers and diseases of viral origin. Recombinant IFN-α from both natural and synthetic genes binds to a common cell surface receptor and induces antiviral activity in a variety of cell lines. When binding to discrete cell surface receptors on target cells, IFN-α induces rapid changes in Jak/Stat phosphorylation, which initiates the Jak/Stat signaling pathway (2). IFN-α signaling also involves production of DAG without an increased intracellular free calcium concentration and the subsequent activation of calcium-independent isoforms of PKC (β and ε) (3). All IFN-α signaling pathways lead to final alterations of gene expression, which mediate their pleiotropic biologic activities.

  1. Stiehm, E.R. et al. (1982) Ann Intern Med 96, 80-93.
  2. Pellegrini, S. et al. (1989) Mol Cell Biol 9, 4605-12.
  3. Pfeffer, L.M. and Colamonici, O.R. (1991) Pharmacol Ther 52, 149-57.

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