Render Target: SSR
Render Timestamp: 2024-11-14T22:45:29.861Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-20 06:23:03.174
Product last modified at: 2024-11-06T13:30:22.960Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Fibronectin/FN1 Antibody #63779

Filter:
  • WB

    Supporting Data

    REACTIVITY M R
    SENSITIVITY Endogenous
    MW (kDa) 300
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

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

    Protocol

    Specificity / Sensitivity

    Fibronectin/FN1 Antibody recognizes endogenous levels of total mouse or rat Fibronectin/FN1 protein.

    Species Reactivity:

    Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp111 of mouse Fibronectin/FN1 protein. Antibodies are purified by peptide affinity chromatography.

    Background

    Fibronectin is a multi-domain extracellular matrix (ECM) protein. The protein uses its different domains to bind distinct ECM components such as collagens, growth factors, and cell surface integrins to carry on its functions (1). Fibronectin has been implicated in many essential biological processes, including tissue repair, fibrosis, and tumor development (1,2). There are many fibronectin isoforms. Plasma fibronectin is synthesized by hepatocytes and exists as a compact, inactive conformation in the bloodstream. It is a major component of fibrin clots. Upon binding to integrins or other cell surface receptors, fibronectin switches to an extended conformation, and exposes its function domains to activated extracellular matrix assembly (3). Fibroblasts, endothelial cells, and many types of cancer cells have also been shown to synthesize cellular fibronectin isoforms. Among them, the EDA or EDB isoforms are particularly highly expressed during fibrosis and cancer development, and are potential diagnostic and therapeutic targets (4-6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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