PAI2, Recombinant, Human (Plasminogen Activator Inhibitor 2, PAI-2, Placental Plasminogen Activator Inhibitor, Monocyte Arg-serpin, Urokinase Inhibitor, Serpin B2, PLANH2, SERPINB2)

PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47kD nonglycosylated intracellular protein which can be induced to be secreted as 60kD glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable, except during pregnancy and in some forms of monocytic leukemia. Secretion of PAI-2 from the placenta normally occurs during the third trimester of pregnancy and accounts for the dramatic increase in PAI-2 levels (up to 250ng/ml), which are maintained at these levels until postpartum, and then rapidly decline. In addition to its vital role in protecting the placenta from degradation by uPA and/or uPA-activated proteases, PAI-2 has been shown to be essential for the prevention of metastatic spread of neck, lung and breast cancers. The beneficial effect of PAI-2 seen in these studies is presumed to stem from its ability to inhibit uPA-dependent cell dissemination. PAI-2 has also been reported to inhibit keratinocyte proliferation, and to participate in the innate immune response during viral infection. Recombinant human PAI-2 is a 415-residue nonglycosylated protein.\n\nBiological Activity:\nDetermined by its inhibitory effect against single chain tPA induced cleavage of a chromogenic substrate in Imidazole Buffer at 37 degrees C. Half maximal inhibition against 1ug/ml of single chain tPA was obtained at a concentration of 1ug/ml.\n\nAA Sequence:\nMEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST EDQMAKVLQFNEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA DKIHSSFRSL SSAINASTGNYLLESVNKLF GEKSASFREE YIRLCQKYYS SEPQAVDFLE CAEEARKKIN SWVKTQTKGKIPNLLPEGSV DGDTRMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREKLNIGYIEDLK AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKMAEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF LSEVFHQAMVDVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH KITNCILFFG RFSSP\n\nQuality Control:\nVerified by N-terminal and Mass Spectrometry analyses (when applicable).\n\nEndotoxin:\n<0.1ng/ug of protein (<1EU/ug).\n\nProtein Content:\nVerified by UV Spectroscopy and/or SDS-PAGE gel.\n\nStorage and Stability:\nStore lyophilized products at -20 degrees C. For reconstituted solutions of most products, we recommend short-term storage at 4 degrees C. For longer term storage the protein solution should be stored with a carrier protein (eg. 0.1% BSA) in working aliquots and stored frozen at -20 degrees C. Additional freeze/thaw cycles may cause some denaturation of the protein.

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