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  2. Protein C - Wikipedia

    en.wikipedia.org/wiki/Protein_C

    Protein C, also known as autoprothrombin IIA and blood coagulation factor XIV, [5]: 6822 [6] is a zymogen, that is, an inactive enzyme.The activated form plays an important role in regulating anticoagulation, inflammation, and cell death and maintaining the permeability of blood vessel walls in humans and other animals.

  3. List of recombinant proteins - Wikipedia

    en.wikipedia.org/wiki/List_of_recombinant_proteins

    The following is a list of notable proteins that are produced from recombinant DNA, using biomolecular engineering. [1] In many cases, recombinant human proteins have replaced the original animal-derived version used in medicine. The prefix "rh" for "recombinant human" appears less and less in the literature.

  4. Protein production - Wikipedia

    en.wikipedia.org/wiki/Protein_production

    The non-pathogenic and gram-negative bacteria, Pseudomonas fluorescens, is used for high level production of recombinant proteins; commonly for the development bio-therapeutics and vaccines. P. fluorescens is a metabolically versatile organism, allowing for high throughput screening and rapid development of complex proteins.

  5. 3K3A-Activated Protein C - Wikipedia

    en.wikipedia.org/wiki/3K3A-Activated_Protein_C

    3K3A-Activated Protein C (3K3A-APC) is an experimental drug for the treatment of stroke developed by ZZ Biotech. [1] It is also being assessed for the treatment of Alzheimer's disease . [ 2 ] It is the subject of RHAPSODY, a phase II trial to determine safety and tolerability.

  6. Category:Recombinant proteins - Wikipedia

    en.wikipedia.org/wiki/Category:Recombinant_proteins

    Pages in category "Recombinant proteins" The following 57 pages are in this category, out of 57 total. This list may not reflect recent changes. ...

  7. Factor IX - Wikipedia

    en.wikipedia.org/wiki/Factor_IX

    The blood coagulation and Protein C pathway.. Factor IX is produced as a zymogen, an inactive precursor.It is processed to remove the signal peptide, glycosylated and then cleaved by factor XIa (of the contact pathway) or factor VIIa (of the tissue factor pathway) to produce a two-chain form, where the chains are linked by a disulfide bridge.

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