Anti-PAI1 Rabbit Antibody [E17P19]

Catalog No.: F3786

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    1:30
    1:10000
    1:60
    Application
    WB, IP, IF, FCM
    Reactivity
    Mouse, Rat, Human
    Source
    Rabbit
    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
    Predicted MW Observed MW
    45 kDa 45 kDa
    *Why do the predicted and actual molecular weights differ?
    The following reasons may explain differences between the predicted and actual protein molecular weight.
    Positive Control Human liver lysate; Mouse placenta; Rat placenta; Human placenta; Mouse liver tissue; Rat lung tissue; HepG2; Hepa1-6; HUVEC
    Negative Control HEK293; NIH/3T3

    Datasheet & SDS

    Biological Description

    Specificity
    PAI1 Rabbit mAb detects endogenous levels of total PAI1 protein.
    Clone
    E17P19
    Synonym(s)
    PAI1, PLANH1, SERPINE1, Plasminogen activator inhibitor 1, PAI, PAI-1, Endothelial plasminogen activator inhibitor, Serpin E1
    Background
    Plasminogen Activator Inhibitor-1 (PAI-1), also known as serpin E1, is a major serine protease inhibitor encoded by the SERPINE1 gene on chromosome 7 and serves as the main physiological blocker of tissue-type (tPA) and urokinase-type (uPA) plasminogen activators, which convert plasminogen to plasmin in fibrinolysis. This 379‑amino‑acid glycoprotein (~48 kDa) has a conserved serpin fold of three β‑sheets, nine α‑helices, and a reactive center loop (RCL) with residues Arg346 and Met347 essential for protease recognition and irreversible inhibition. In its active state, PAI‑1 is metastable and can spontaneously shift to an inactive latent form unless stabilized by vitronectin. It also influences extracellular matrix remodeling, cell adhesion, migration, angiogenesis, and inflammation, and is produced by endothelial cells, hepatocytes, adipocytes, and some neurons. High PAI‑1 levels are linked to thrombosis, fibrosis, obesity, insulin resistance, cancers, vascular stiffness, and senescence, and in the CNS it affects neuroinflammation and amyloid‑β clearance, relating to Alzheimer’s and Parkinson’s disease. As an acute‑phase reactant, its rise during injury or infection can become harmful if chronically elevated, and genetic variations in SERPINE1 affect its expression and disease risk.
    References
    • https://pubmed.ncbi.nlm.nih.gov/33415130/
    • https://pubmed.ncbi.nlm.nih.gov/20626406/

    Tech Support

    Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

    Handling Instructions

    Tel: +1-832-582-8158 Ext:3
    If you have any other enquiries, please leave a message.

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