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Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

c-Fos (E2I7R) XP® Feline Chimeric mAb #42157

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  • IF

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Feline chimeric IgG1
    Application Key:
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Description

    This Cell Signaling Technology® antibody retains the antigen-binding Fab regions of the original parent host sequence from which it is engineered. This antibody is expected to exhibit the same species cross-reactivity as c-Fos (E2I7R) XP® Rabbit mAb #31254.

    Product Usage Information

    Application Dilution
    Immunofluorescence (Frozen) 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    c-Fos (E2I7R) XP® Feline Chimeric mAb recognizes endogenous levels of total c-Fos protein. This antibody does not cross-react with other Fos proteins, including FosB and FRA1. This antibody non-specifically stains fixed, frozen mouse spleen by immunofluorescence.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    This recombinant chimeric antibody is engineered from c-Fos (E2I7R) XP® Rabbit mAb #31254 according to animal-free protocols. The chimeric antibody retains its antigen-binding Fab regions from the original rabbit monoclonal antibody but contains a feline-derived Fc domain. When multiplexing, Fc-directed rabbit secondaries are required to detect rabbit-host primary antibodies.

    The parent antibody, c-Fos (E2I7R) XP® Rabbit mAb #31254, is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala286 of human c-Fos protein.

    Background

    The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), which lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer, and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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