According to this method, increased amounts of both recombinant factor VIII and native factor VIII are purified from cells producing factor VIII.
The process is used for the purification of recombinant compositions of coagulation factor, particularly recombinant Factor VIII.
The present invention relates to a recombinant factor VIII that includes one or more mutations that result in enhanced stability of both factor VIII and factor VIIIa.
Provided are liquid and lyophilized recombinant Factor VIII formulations, including formulations for polymer-conjugated FVIII such as PEGylated Factor VIII.
The factor VIII is suitably a highly purified recombinant factor VIII, and preferably a deletion derivative thereof, which can be used for the manufacture of a medicament for subcutaneous administration.
The successful cloning of the factor VIII gene in 1984 was a major breakthrough, allowing production of recombinant human factor VIII (r factor VIII).
The successful cloning of the factor VIII gene in 1984 was a major breakthrough, allowing production of recombinant human factor VIII.
Methods of making and using the recombinant factor VlIl, and pharmaceutical compositions containing the same are also disclosed.
In 1992, the first recombinant factor VIII product was approved by the FDA.
The cumulative incidence of high titre inhibitors was 18.6 per cent with plasma-derived factor VIII and 28.4 per cent with recombinant factor VIII.
In 1997, the first recombinant factor IX product was granted FDA approval.
1992 – The first recombinant factor VIII product was approved by the FDA.
Inhibitors are a treatment challenge for both blood-derived and recombinant factor VIII medicines.
Conjugates containing a substance with coagulant activity, such as recombinant factor VIII, and non-antigenic polymers, such as poly(ethylene glycol), are disclosed (as shown in the figure).
A number of novel recombinant factor VIII products have been developed in recent years, including some with an extended half-life.
The disclosure further relates to a process of producing a functional recombinant Factor VIII protein by reconstituting the Heavy chain and Light chain produced using said Pichia pastoris expression system.
The present invention relates to the functional expression of recombinant factor VIII (r FVIII) in cells and in particular to its stable expression and excretion from cells in in vitro and/or in vivo applications.
The present invention further relates to an isolated nucleic acid molecule that encodes the recombinant factor VIII, as well as DNA expression systems and host cells containing the isolated nucleic acid molecule.
The present disclosure relates specifically to a process of producing heavy chain peptide and/or light chain peptide of recombinant Factor VIII protein using Pichia pastoris expression system.
There is provided inter alia a cell culture medium for recombinant Factor VIII production characterized in that the culture medium contains calcium ions and a strong ligand such as EDTA.
Requêtes fréquentes français :1-200, -1k, -2k, -3k, -4k, -5k, -7k, -10k, -20k, -40k, -100k, -200k, -500k, -1000k,
Requêtes fréquentes anglais :1-200, -1k, -2k, -3k, -4k, -5k, -7k, -10k, -20k, -40k, -100k, -200k, -500k, -1000k,
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