Render Target: STATIC
Render Timestamp: 2024-12-20T11:02:12.620Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:59:54.635
Product last modified at: 2024-11-22T15:15:09.489Z
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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.

ITM2C/Bri3 (F3X8Z) Rabbit mAb #88436

Filter:
  • WB
  • IF

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 31, 27
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunofluorescence (Frozen) 1:100 - 1:400
    Immunofluorescence (Immunocytochemistry) 1:200 - 1:800

    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

    ITM2C/Bri3 (F3X8Z) Rabbit mAb recognizes endogenous levels of total ITM2C/Bri3 protein. This antibody detects full-length ITM2C/Bri3 (~31 kDa) and processed ITM2C/Bri3 without the C-terminal peptide (~27 kDa) by western blot.


    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human ITM2C/Bri3 protein.

    Background

    The BRI gene family comprises at least three members, BRI1/ITM2A, BRI2/ITM2B, and BRI3/ITM2C, which encode three type II transmembrane glycoproteins BRI1, BRI2, and BRI3, respectively. BRI3 expression is highest in the brain but the protein is also expressed in plasmacytoid dendritic cells, appendix, peripheral blood leukocytes, bone marrow, and fetal liver (1). BRI2 and BRI3 have been reported to negatively regulate amyloid β (Aβ) production by binding to Aβ precursor protein (APP) and inhibiting its processing by secretases. Both proteins mask the cleavage sites of α- and β-secretase on APP. However, unlike BRI2, the binding of BRI3 to the β-secretase cleaved APP C-terminal fragment is negligible (2,3). More recently, the BRI3/ITM2C gene signature has been identified as a potential marker for the early detection of colorectal cancer (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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