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. uPA 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of PAI-2 of mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 61-130 mapping near the N-terminus of PAI-2 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 61-130 mapping near the N-terminus of PAI-2 of mouse origin