SERPINE1 Antibody - #BF0086
*The optimal dilutions should be determined by the end user.
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# BF0086, RRID:AB_2833974.
Clade E; Endothelial plasminogen activator inhibitor; Nexin; PAI 1; PAI; PAI-1; PAI1_HUMAN; PLANH1; Plasminogen activator inhibitor 1; Plasminogen activator inhibitor type 1; Serine (or cysteine) proteinase inhibitor; Serine (or cysteine) proteinase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1; Serpin E1; Serpin peptidase inhibitor clade E (nexin plasminogen activator inhibitor type 1) member 1; Serpin peptidase inhibitor clade E; Serpine 1; SERPINE1;
Purified recombinant fragment of human SERPINE1 expressed in E. Coli.
Expressed in endothelial cells (PubMed:2430793, PubMed:3097076). Found in plasma, platelets, and hepatoma and fibrosarcoma cells.
PTMs - P05121 As Substrate
Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair. It is involved in cellular and replicative senescence. Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis.
Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.
Expressed in endothelial cells. Found in plasma, platelets, and hepatoma and fibrosarcoma cells.
Forms a heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Interacts with PPP1CB. In complex with PLAU/uPA, interacts with PLAUR/uPAR. Interacts with SORL1 and LRP1, either alone or in complex with PLAU; these interactions are abolished in the presence of LRPAP1/RAP. The ternary complex composed of PLAUR-PLAU-PAI1 also interacts with SORL1. Also interacts with SORL1, when complexed to PLAT/tPA.
Belongs to the serpin family.
· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).
Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.
For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.