SERPINE2,Glia-derived nexin,GDN,Peptidase inhibitor 7,PI-7,Protease nexin 1,PN-1,Serpin E2,SerpinE2,PI7
Human Serpin E2 / PN1 Protein (Human Serpin E2, His Tag) Ser 20 - Pro 397 (Accession # P07093-2) was produced in human 293 cells (HEK293) at ACROBiosystems.
Human Serpin E2, His Tag 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. The reducing (R) protein migrates as 45-48 kDa in SDS-PAGE due to glycosylation.
Less than 1.0 EU per μg by the LAL method.
>92% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 20 mM NaAc, 100 mM NaCl, PH6.5. Normally Mannitol or Trehalose are added as protectants before lyophilization.
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See Certificate of Analysis for reconstitution instructions and specific concentrations.
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).
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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