Serpin E1/PAI-1 Products

Description

PAI-1 and PAI-2 (for plasminogen activator inhibitor-1 and -2) are members of the serpin serine proteinase inhibitor family. PAI-1 and PAI-2 have been shown to regulate uPA (urokinase-type plasminogen activator) and tPA (tissue plasminogen activator), resulting in the inhibition of proteolytic activity. Members of the serpin family generally complex with their target proteinases, then disassociate slowly into cleaved species that fold into stable inactive forms. PAI-1 can fold into the inactive state without cleavage, resulting in the latent form of PAI-1. Activity can be restored to the latent form of PAI-1 through denaturation and renaturation. PAI-2 occurs in secreted and cytosolic forms through facultative polypeptide translocation. uPA is a serine proteinase that is a member of the trypsin family. It is responsible for the cleavage of plasminogen at the Arg-Val bond to produce plasmin. uPA consists of two chains designated A and B. The A chain can be cleaved, resulting in low and high molecular mass forms of uPA.

Bioinformatics

Uniprot	AAH10860 Human NM_000602 Human NP_000593 Human NP_000593.1 Human NP_000593.1. Human P05121 Human
Product By Gene ID	5054
Alternate Names	Endothelial plasminogen activator inhibitor PAI1PAI-1 PAISerpin E1 PLANH1plasminogen activator inhibitor 1 serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 1 serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 1

Research Areas for Serpin E1/PAI-1

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Cancer