Render Target: STATIC
Render Timestamp: 2024-11-07T09:39:43.035Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-20 06:15:46.287
Product last modified at: 2024-08-07T13:30:09.280Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Villin-1 (R814) Antibody #2369

Filter:
  • WB

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 95
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    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

    Villin-1 (R814) Antibody recognizes endogenous levels of total villin-1 protein.

    Species Reactivity:

    Human, Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human villin-1. Antibodies are purified using protein A and peptide affinitty chromatography.

    Background

    Villin is a member of the gelsolin family of calcium-regulated actin-binding proteins. Unlike the ubiquitously expressed gelsolin, villin expression is restricted to simple epithelia of the gastrointestinal and urogenital tracts. It is localized to the apical cytoplasm and brush borders of these cells. Villin functions in the regulation of actin dynamics in the apical epithelium, capping, nucleating and/or severing actin filaments in a calcium-dependent manner and regulating cell shape in response to external stimuli (1,2). Phosphorylation of villin at Tyr60, 81, and 256 may be involved in the regulation of cell migration (3). Expression of villin is increased in colorectal cancers (4), and villin-1 function appears to be involved in progressive cholestasis and hepatic failure (5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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