Render Target: STATIC
Render Timestamp: 2025-02-07T12:12:41.176Z
Commit: 1bba917eefc12d62e72a522121e2774ffbd0ee36
XML generation date: 2024-09-30 01:58:29.932
Product last modified at: 2025-01-17T14:30:09.567Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

GUCY2C (E1Q6S) Rabbit mAb #29881

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 145, 130
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunofluorescence (Immunocytochemistry) 1:50 - 1:200

    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

    GUCY2C (E1Q6S) Rabbit mAb recognizes endogenous levels of total GUCY2C protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human GUCY2C protein.

    Background

    Guanylyl cyclase C (GUCY2C) is a type I transmembrane glycoprotein whose expression in normal tissue is largely restricted to the apical membranes of polarized epithelial cells of the intestine (1,2). The guanylyl cyclase activity within the intracellular domain of GUCY2C is activated by binding exogenous bacterial enterotoxins and the endogenous peptide hormone agonists, guanylin and uroguanylin, which facilitates production of the second messenger cGMP (3-5). GUCY2C signaling plays a critical role in regulating the metabolism, proliferation, and differentiation of intestinal epithelial cells. These processes are critical for epithelial barrier renewal, water, and ion balance (6-8). Research studies have shown that the GUCY2C signaling axis functions to suppress intestinal tumorigenesis, in part, by restraining AKT activity (9,10). Lesions in the GUCY2C signaling axis that frequently contribute to cellular transformation are associated with a loss of expression of its endogenous ligands, which promotes a compensatory increase in GUCY2C expression. Indeed, GUCY2C expression is maintained in a high percentage of primary and metastatic human colorectal tumors, which has raised interest in therapeutically targeting this receptor (11,12).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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