Abstract: A connection system for connecting a safety razor handle (50) to a replaceable blade cartridge (10), comprising: a cartridge connecting structure (120) attached to the replaceable blade cartridge (10); and a handle connecting structure (102) attached to the safety razor handle (50) and configured to be brought into engagement with the cartridge connecting structure (120) along a connection axis, wherein the handle connecting structure (102) comprises a lever (112) mounted to a body (103), the lever (112) having a user end (113) to be actuated by a user, a working end (114), and a rotation axis (115) about which the lever (112) is rotatable with respect to the body (103), the rotation axis (115) being situated between the user end (113) and the working end (114), and the working end (114) of the lever (112) is configured to exert a pushing force on the cartridge connecting structure (120) when the lever (112) is rotated by actuation of the user end (113), to eject the cartridge connecting structure (120) from

Abstract: A blade unit and a lubrapad for attachment to a handle of a safety razor, the blade unit comprising: a blade housing and a plurality of blades disposed within the blade housing to expose respective cutting edges suitable for shaving; the blade housing including a guard in front of the cutting edges and a cap to the rear of the cutting edges; and the lubrapad comprising: a lubrapad body comprising solid lubricating material and provided separately from the blade unit, extending along the guard and in front of the guard, the body having a greatest width and/or depth in the blade direction at the guard, the body width and/or depth reducing in a smooth convex curve away from the guard to a curved front portion of the body; wherein the blade unit and lubrapad are arranged to move independently with respect to each other.

Abstract: A safety razor handle comprising: a handle body (50) and a cartridge attachment means (59); wherein the handle body is bulbous in two orthogonal directions, widening away from an end surface (52) towards the centre of the body.

Abstract: A safety razor handle comprising: an underneath surface portion facing the skin of the user in use and comprising an attachment means for attachment to a blade unit; a front surface portion facing in the opposite direction from the shaving direction in use; a rear surface portion facing in the shaving direction in use; a top surface portion and side surface portions, one directed to either side of the blade length in use; wherein the top surface portion, underneath surface portion and side surface portions together form a continuous smooth surface (which is a substantially cylindrical or substantially ellipsoid or substantially partially spherical surface; and wherein: the distance between the front surface portion and rear surface portion is between one third and three times, preferably between a half and twice, the largest dimension of the largest cross section through the continuous smooth surface.

Abstract: A safety razor (100) comprising; a handle body (50) with a substantially flat end surface (52) and a side surface (58); and a cartridge (10) attached to the side surface, wherein: when the flat end surface (52) is in contact with a horizontal plane, the safety razor is in a stable position of rest, the flat end surface forming the safety razor's only region of contact with the plane and elevating the cartridge (10) above the plane.

Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Abstract: The present disclosure is directed to glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations comprising the conserved amino acid motif (“QVWxKDS”) were found to be compatible with glycosyltransferase enzymatic activity, particularly in a human sialyltransferase (hST6Gal-I). Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Abstract: The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Abstract: The current invention comprises a method for producing an immunoglobulin or immunoglobulin fragment with defined glycostructure comprising the following steps: a) providing an affinity chromatography column eluate containing the immunoglobulin or immunoglobulin fragment, b) incubating the affinity chromatography column eluate with (?1,3)galactosidase of plant origin, e.g. from green coffee beans (EC 3.2.1.22), c) applying the incubated affinity chromatography column eluate to a protein A chromatography material and recovering the immunoglobulin or immunoglobulin fragment from the protein A chromatography material and thereby producing an immunoglobulin or immunoglobulin fragment with defined glycostructure.

Abstract: The current invention comprises a method for producing an immunoglobulin or immunoglobulin fragment with defined glycostructure comprising the following steps: a) providing an affinity chromatography column eluate containing the immunoglobulin or immunoglobulin fragment, b) incubating the affinity chromatography column eluate with (?1,3)galactosidase of plant origin, e.g. from green coffee beans (EC 3.2.1.22), c) applying the incubated affinity chromatography column eluate to a protein A chromatography material and recovering the immunoglobulin or immunoglobulin fragment from the protein A chromatography material and thereby producing an immunoglobulin or immunoglobulin fragment with defined glycostructure.