Human CellExp Serpin E2 / PN1, human recombinant protein
SERPINE2, Glia-derived nexin, GDN, Peptidase inhibitor 7, PI-7, Protease nexin 1, PN-1, Serpin E2, S
|Calculated MW||This protein is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 42.7 kDa. The predicted N-terminus is Ser 20. DTT-reduced Protein migrates as 45-48 kDa in SDS-PAGE due to glycosylation.|
|Other Names||SERPINE2, Glia-derived nexin, GDN, Peptidase inhibitor 7, PI-7, Protease nexin 1, PN-1, Serpin E2, SerpinE2, PI7|
|Target/Specificity||Serpin E2 / PN1|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in PBS, pH 7.4. Do not vortex.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in 20 mM NaAc, 100 mM NaCl, pH 6.5. Normally Mannitol or Trehalose are added as protectants before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
SERPINE2 is also known as Glia-derived nexin (GDN), Peptidase inhibitor 7 (PI7), Protease nexin 1(PN1). SERPINE2 is a secreted glycoprotein which belongs to the serpin family. SerpinE1 is the primary physiological inhibitor of the two plasminogen activators urokinase (uPA) and tissue plasminogen activator (tPA). PAI-1 / GDN is also implicated in adipose tissue development. It suggests that PAI-1 inhibitors serve in the control of atherothrombosis. Defects in Serpin E1 / PN1 are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency) which is characterized by abnormal bleeding due to SerpinE1 defect in the plasma.
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McGrogan M.,et al.Biotechnology (N.Y.) 6:172-177(1988).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Hillier L.W.,et al.Nature 434:724-731(2005).
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