Render Target: STATIC
Render Timestamp: 2024-12-20T11:39:37.437Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-12-17 23:02:08.398
Product last modified at: 2024-12-18T09:00:16.607Z
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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.

PIGR (F9A8F) Rabbit mAb #59629

Filter:
  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Flow Cytometry (Fixed/Permeabilized) 1:200 - 1:800
    Flow Cytometry (Live) 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

    PIGR (F9A8F) Rabbit mAb recognizes endogenous levels of total PIGR protein. This antibody reacts with PIGR and secretory component (SC).

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val28 of human PIGR protein.

    Background

    Polymeric immunoglobulin receptor (PIGR) is a highly glycosylated type I membrane protein that mediates transcytosis of immunoglobulin A (IgA) and immunoglobulin M (IgM) across epithelial cells at mucosal surfaces (1,2). The extracellular portion of PIGR is made up of six domains. Domains 1 through 5 are composed of Ig-like domains that bind to IgA dimers or IgM pentamers, and domain 6 contains a conserved proteolytic cleavage site (3). PIGR binds Ig made in the lamina propria via the joining (J) chain. It undergoes clathrin-mediated endocytosis and is further transcytosis through the epithelial cell to the mucosa (4). PIGR then undergoes endoproteolytic cleavage and disassociates from the membrane domain to form the secretory component (SC) and associated Ig, or secretory Ig (SIg) (5). SC enhances SIg stability by resisting proteolytic degradation and can act as a non-specific microbial scavenger, leading to the sequestration of bacteria in the mucus layer (6,7). PIGR expression and SIg secretion are induced by microbial factors, including LPS, butyrate, and dsRNA, and by pro-inflammatory cytokines like IFN-γ, TNF-α, IL-1, and IL-17 (8). PIGR is expressed aberrantly in cancers and has been proposed as a biomarker with prognostic value and as a therapeutic target (9-11). 
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