6 results about "Aspartyl Proteinases" patented technology

Anti-VEGF proteins, including the VEGF trap protein aflibercept, can be manufactured to have a low content of an aspartyl protease (e.g., a low content of cathepsin D), for example, less than 1 ppm of the aspartyl protease.

Anti-VEGF proteins including the VEGF trap protein aflibercept can be produced to have a low level of an aspartyl protease (e.g., a low level of cathepsin D), such as less than 1 ppm of the aspartyl protease.

The present invention provides a novel antibody fragment based antifungal conjugate selectively targeting Candida spp. comprising of at least one antimicrobial peptide at one end of the conjugate, more particularly, human Histatin-5; an antibody fragment at the other end of the conjugate, specific against Candida spp. enolase, a virulence factor protease and biofilm specific antigen of Candida spp.; at least one signal protease cleavage sequence susceptible to cleavage by virulent protease secreted by Candida spp., secreted aspartyl proteinase-1 (SAP1); and at least one flexible polypeptide linker. The signal protease cleavage sequence and the flexible polypeptide linker are in tandem with each other and placed in between the antimicrobial peptide and the antibody. The in vitro MIC-99 of the conjugate against Candida spp., is in the range of 0.2-0.3 μM, more specifically, 0.25 μM or 250 nM.

Anti-VEGF proteins including the VEGF trap protein aflibercept can be produced to have a low level of an aspartyl protease (e.g., a low level of cathepsin D), such as less than 1 ppm of the aspartyl protease.

Anti-VEGF proteins including the VEGF trap protein aflibercept can be produced to have a low level of an aspartyl protease (e.g., a low level of cathepsin D), such as less than 1 ppm of the aspartyl protease.

The present invention relates to food products comprising recombinant polypeptide compositions that are substantially free of aspartyl protease-like activity. The invention also relates to compositions comprising recombinant milk polypeptides and that are substantially free of aspartyl protease-like activity; and methods and tools for manufacture of such compositions.