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PLVAP/PV-1 Antibody [E23J22]

Cat.No.: F2799

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    1:1000
    1:10000
    Application
    IHC, IF, FCM
    Reactivity
    Mouse
    Source
    Rat Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years

    Datasheet & SDS

    Biological Description

    Specificity
    PLVAP/PV-1 Antibody [E23J22] detects endogenous levels of total PLVAP/PV-1 protein.
    Clone
    E23J22
    Synonym(s)
    Pv1; Plasmalemma vesicle-associated protein; MECA-32 antigen; Plasmalemma vesicle protein 1; PV-1
    Background
    PLVAP (PV-1, plasmalemma vesicle-associated protein) is a type II transmembrane glycoprotein selectively expressed in fenestrated endothelia of kidney glomeruli, intestinal villi, liver sinusoids, and tumor neovasculature, but absent from the blood-brain barrier and continuous vessels, that organizes stomatal and fenestral diaphragms via its ~390-residue C-terminal extracellular coiled-coil domain. This domain forms rigid, parallel α-helical homodimers stabilized by five interchain disulfide bonds (Cys142, Cys153, Cys178, Cys199, Cys224), radiating as 8–10 spoke-like fibers spanning caveolar necks or fenestrae with precise 10–15 nm geometry. Functioning as a molecular sieve, PLVAP selectively restricts plasma protein transcytosis through caveolae and transendothelial channels, establishing a cutoff that allows passage of albumin and IgG while blocking larger complexes. VEGF/PI3K/p38MAPK signaling transcriptionally induces PLVAP during angiogenesis to widen caveolar openings and increase diaphragm density, which paradoxically enhances paracellular leakage via endothelial contractility. Genetic ablation of PLVAP results in 2–3-fold enlarged caveolae, loss of diaphragms, protein-losing enteropathy, hypoproteinemia, hypertriglyceridemia, and neonatal lethality from circulatory collapse, underscoring its essential role in maintaining basal permeability restriction. PLVAP is upregulated by hypoxia and VEGF, marking leaky tumor microvasculature that facilitates metastasis, and mediates vasogenic edema and leukocyte diapedesis in ischemia and sepsis.
    References
    • https://pubmed.ncbi.nlm.nih.gov/36996108/
    • https://pubmed.ncbi.nlm.nih.gov/15155804/

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