Abstract: A modified uricase is described herein, as well as a method of reducing a level of uric acid by contacting a medium with the modified uricase. The modified uricase comprises a uricase polypeptide crosslinked by at least one bifunctional linking moiety that comprises a poly(alkylene glycol) moiety. A molecular weight of the bifunctional linking moiety is from about 1.5 kDa to about 4 kDa, and/or the modified uricase comprises a plurality of polypeptides having the amino acid sequence SEQ ID NO: 2. Further described is a polypeptide having the amino acid sequence SEQ ID NO: 2. A process of preparing the modified uricase is also described, comprising contacting the polypeptide with a crosslinking agent that comprises a poly(alkylene glycol) moiety and at least two aldehyde groups, to obtain a conjugate; and contacting the conjugate with a reducing agent.

Abstract: A modified DNase protein is described herein as well as pharmaceutical compositions comprising same, the modified DNase protein comprising a DNase polypeptide attached to at least two poly(alkylene glycol) moieties. Further described herein is a process of preparing a modified DNase protein, the process comprising: contacting the polypeptide with an agent that comprises a poly(alkylene glycol) attached to an aldehyde group, to obtain a conjugate of the polypeptide and the agent; and contacting the conjugate with a reducing agent.

Abstract: DICER-liker knock-out plant cells are provided. Accordingly, there is provided an isolated plant cell in suspension comprising loss of function mutations in all alleles of at least two genes selected from the group consisting of DCL2, DCL4, RDR1, RDR2 and RDR6 in said plant cell. Also provided are methods of abolishing expression and/or activity of at least two genes selected from the group consisting of DCL2, DCL4, RDR1, RDR2 and RDR6 in a plant cell.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: A nucleic acid construct is disclosed which is removable after transformation. Methods of using same are disclosed as well.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: A plant produced chimeric polypeptide is provided. The plant produced chimeric polypeptide comprising: (i) a first domain which comprises a TNF Alpha binding domain of a TNF receptor, and (ii) a second domain which comprises an Fc domain of an immunoglobulin, wherein the first domain and the second domain are N-terminally to C-terminally respectively sequentially translationally fused and wherein the chimeric polypeptide specifically binds TNF Alpha.

Abstract: Methods of treating Fabry disease via administration of stabilized plant recombinant human alpha galactosidase protein comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety, and unit dosages of protein are disclosed herein. The disclosed protocols are safe, have greater than 2 week intervals between administrations and exhibit important improvement in patient's disease parameters, in terms of reduced Gb3 accumulation, pain and GI parameters, kidney and cardiac stabilization in the clinical setting.

Abstract: A reusable, disposable device for culturing plant tissues or cells including a non-rigid container having dimensions and gas exchange ports designed for maintaining oxygen saturation and shear forces suitable for culturing plant tissue or cells in 400 liters or more of culture medium is provided. Also provided are methods for producing a catalytically active human recombinant protein in a plant cell, using the disposable device of one of the embodiments of the instant specification.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: A plant produced chimeric polypeptide is provided. The plant produced chimeric polypeptide comprising: (i) a first domain which comprises a TNF Alpha binding domain of a TNF receptor, and (ii) a second domain which comprises an Fc domain of an immunoglobulin, wherein the first domain and the second domain are N-terminally to C-terminally respectively sequentially translationally fused and wherein the chimeric polypeptide specifically binds TNF Alpha.

Abstract: A plant produced chimeric polypeptide is provided. The plant produced chimeric polypeptide comprising: (i) a first domain which comprises a TNF Alpha binding domain of a TNF receptor, and (ii) a second domain which comprises an Fc domain of an immunoglobulin, wherein the first domain and the second domain are N-terminally to C-terminally respectively sequentially translationally fused and wherein the chimeric polypeptide specifically binds TNF Alpha.

Abstract: A method of treating a TNF Alpha associated medical condition selected from the group consisting of obesity, metabolic syndrome, diabetes and a liver disease or disorder is provided. The method comprising enterally administering to a subject in need thereof a therapeutically effective amount of plant cells expressing a TNF Alpha polypeptide inhibitor, thereby treating the TNF Alpha associated medical condition.

Abstract: A plant produced chimeric polypeptide is provided. The plant produced chimeric polypeptide comprising: (i) a first domain which comprises a TNF Alpha binding domain of a TNF receptor, and (ii) a second domain which comprises an Fc domain of an immunoglobulin, wherein the first domain and the second domain are N-terminally to C-terminally respectively sequentially translationally fused and wherein the chimeric polypeptide specifically binds TNF Alpha.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Nucleic acid expression constructs are provided and, more particularly, nucleic acid constructs for expression of human alpha-galactosidase in plant cells, cells expressing the nucleic acid construct, producing the human alpha-galactosidase and uses thereof.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: An inhalable pharmaceutical composition for pulmonary administration comprising human DNase I and a liquid carrier and, more particularly, but not exclusively, to methods, liquid pharmaceutical inhalation devices and systems for the therapeutic use thereof are provided.