Recombinant Human Serpin A5/Protein C Inhibitor (C-6His)(Discontinued)
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| Amount : | 50 µg |
| Content : | Lyophilized from a 0.2 µm filtered solution of 20mM MES, 150mM NaCl, pH 5.5. |
| Storage condition : | 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. |
| AA sequence : | HRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQNIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRPVDHHHHHH |
Source: Human Cells.
MW :44.7kD.
Recombinant Human Serpin A5 is produced by our Mammalian expression system and the target gene encoding His20-Pro406 is expressed with a 6His tag at the C-terminus. Serpin A5 is a member of the human Serpin superfamily consists of at least 35 members. It is synthesized in the liver and has been detected in saliva, cerebral spinal fluid, amniotic fluid, tears and semen. As a potent inhibitor of the protein C anticoagulant pathway at the levels of both zymogen activation and enzyme inhibition, Serpin A5 additionally inhibits a variety of serine protease including thrombin, factor Xa, several kallekreins and acrosin. It plays a critical role in the processes of blood of blood coagulation and fertilization. Serpin A5 also inhibits urinary plasminogen activator (uPA), a mediator of tumor cell invasion, and regulates tumor growth and metastasis by inhibiting angiogenesis. Furthermore, recent studies have identified PCI as a potent and direct inhibitor of activated HGFA (hepatocyte growth factor activator), suggesting a novel function in the regulation of tissue repair and regeneration. Similar to Serpins C1 and D1, the thrombin inhibitory activity of serpinA5 is enhanced by heparin.
MW :44.7kD.
Recombinant Human Serpin A5 is produced by our Mammalian expression system and the target gene encoding His20-Pro406 is expressed with a 6His tag at the C-terminus. Serpin A5 is a member of the human Serpin superfamily consists of at least 35 members. It is synthesized in the liver and has been detected in saliva, cerebral spinal fluid, amniotic fluid, tears and semen. As a potent inhibitor of the protein C anticoagulant pathway at the levels of both zymogen activation and enzyme inhibition, Serpin A5 additionally inhibits a variety of serine protease including thrombin, factor Xa, several kallekreins and acrosin. It plays a critical role in the processes of blood of blood coagulation and fertilization. Serpin A5 also inhibits urinary plasminogen activator (uPA), a mediator of tumor cell invasion, and regulates tumor growth and metastasis by inhibiting angiogenesis. Furthermore, recent studies have identified PCI as a potent and direct inhibitor of activated HGFA (hepatocyte growth factor activator), suggesting a novel function in the regulation of tissue repair and regeneration. Similar to Serpins C1 and D1, the thrombin inhibitory activity of serpinA5 is enhanced by heparin.
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 ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Secreted |
| Post transnational modification: | Proteolytically cleaved. Inhibition of proteases is accompanied by formation of a stable enzyme-inhibitor complex and by degradation of the serpin to lower molecular weight derivatives. Proteolytically cleaved at the N-terminus; inhibits slightly the heparin- and thrombomodulin-enhanced rates of thrombin inhibition. |
| Tissue Specificity: | Predominantly expressed in the epithelium of seminal vesicles. Expressed in the proximal tubular epithelium of the kidney. Expressed in the superficial and more differentiated epidermal keratinocytes of the skin. Expressed in megakaryocytes and platelets. Expressed poorly in kidney tumor cells compared to non tumor kidney tissues. Expressed in spermatozoa. Present in very high concentration in seminal plasma. Present in high concentration in plasma, synovial and Graaf follicle fluids. Present in low concentration in breast milk and in amniotic fluids. Present in very low concentration in urine, cerebrospinal fluids, saliva and tears (at protein level). Strongly expressed in liver. Expressed in kidney, spleen, pancreas, skeletal muscle, heart, testes, ovary, interstitial Leydig cells, epididymal glands, seminal vesicles and prostate. |
| BioGrid: | 111135. 24 interactions. |
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