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PAI1 Mouse anti-Human, Mouse, Rat, Clone: MA-55F4C12, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA140225

Catalog No. 01-676-565

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MA1-40225 detects PAI-1 from human, mouse, and rat samples. MA1-40225 has been successfully used in functional assays and ELISA applications. The MA1-40225 immunogen is human PAI-1. Endotoxin <24 EU/mg. The epitope of MA1-40225 is within the stretch of 29 amino acids in PAI-1 (region Glu128 -Ala131). Glu128, Val129, Glu130, Arg131 and Lys154 are the major determits. All five residues act cooperatively in the binding to MA-55F4C12 and constitute the epitope. The epitope of the antibody does not cover the complete alpha-helix F and turn connecting alpha-helix F and beta-strand s3A, but is restricted to the hinge region between alpha-helix F and the main part of the PAI-1 molecule. MA1-40225 is a ‘switching’ antibody, capable of inducing a non-inhibitory substrate form of PAI-1. The antibody cross reacts with rat and mouse PAI-1.

PAI1 (plasminogen activator inhibitor 1) belongs to serine protease inhibitor superfamily, and is the principal inhibitor of tissue-type and urokinase-type plasminogen activators (tPA and uPA). Platelets are the main source of the circulating PAI11, but it is synthesized and secreted by many tissue and cell types, including fibroblasts, smooth muscle cells, endothelial cells, hepatocytes, and inflammatory cells. Expression of PAI11 can be regulated at the transcriptional level by many factors including growth factors, cytokines, hormones, inflammatory factors, glucose or lipid metabolites, vascular tone regulating factors, chemicals, and other environmental or physical factors. The active conformation PAI-1 inhibits its target proteinases by the formation of a stable, inactive complex. Although PAI-1 is synthesized as an active molecule, it converts spontaneously to an inactive, latent form that can be partially reactivated by denaturing agents. In addition, a third conformation reacting as a non-inhibitory substrate towards various target proteinases has been identified. PAI1 is present at increased levels in various disease states, and has been linked to an increased occurrence of thrombosis in obesity, thrombophilia and the metabolic syndrome. Defects in PAI-1 are characterized by abnormal bleeding. PAI1 mediates inhibition of fibrinolysis by inhibiting the activity of plasminogen activator, and may promote neuronal survival. Other defects in PAI1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency). Alternatively spliced transcript variants encoding different isoforms of PAI1 have been found.


0.1 mg/mL
PBS with 0.1% BSA and no preservative
P05121, P22777, P20961
100 μg
4° C
18787, 24617, 5054
ELISA, Functional Assay
Human PAI-1.
Human, Mouse, Rat


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