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C537
Recombinant Human Plasminogen Activator Inhibitor 1/PAI1
10ug
1200
1080
现货
国产
-
C537
Recombinant Human Plasminogen Activator Inhibitor 1/PAI1
50ug
3520
3168
现货
国产
-
C537
Recombinant Human Plasminogen Activator Inhibitor 1/PAI1
500ug
12320
11088
现货
国产
-
C537
Recombinant Human Plasminogen Activator Inhibitor 1/PAI1
1mg
17600
15840
现货
国产
-
C537
Recombinant Human Serpin E1/PAI-1
10ug
1200
1080
现货
国产
-
C537
Recombinant Human Serpin E1/PAI-1
50ug
3520
3168
现货
国产
-
C537
Recombinant Human Serpin E1/PAI-1
500ug
12320
11088
现货
国产
-
C537
Recombinant Human Serpin E1/PAI-1
1mg
17600
15840
现货
国产
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Catalog# C537 Source HEK293 Description Recombinant Human Serpin E1 produced by transfected human cells is a secreted protein with sequence (Val24-Pro402) of Human SERPINE1 fused with a polyhistidine tag at the C-terminus. Names Plasminogen Activator Inhibitor 1, PAI, PAI-1, Endothelial Plasminogen Activator Inhibitor, Serpin E1, SERPINE1, PAI1, PLANH1 Accession # P05121 Formulation Lyophilized from a 0.2 μm filtered solution of 20mM HAc-NaAc, 150mM NaCl, pH 4.0 Shipping The product is shipped at ambient temperature. Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Endotoxin Less than 0.1 ng/µg (1 IEU/µg). Amino Acid Sequence VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFK IDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVE RARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGS TVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLIS HWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVK IEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEPLDHHHHHHBackground Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. They are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpin E1 is a secreted protein which belongs to the Serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Defects in SERPINE1 are characterized by abnormal bleeding due to Serpin E1 defect in the plasma. High concentrations of Serpin E1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.