Antibodies that include a sulfatase motif-containing tag in a constant region of an immunoglobulin (Ig) light chain polypeptide are disclosed. The sulfatase motif can be converted by a formylglycine-generating enzyme (FGE) to produce a formylglycine (fGly)-modified Ig light chain polypeptide. An fGly-modified Ig light chain polypeptide of the antibody can be covalently and site-specifically bound to a moiety of interest to provide an antibody conjugate. The disclosure also encompasses methods of production of such tagged Ig light chain polypeptides, fGly-modified Ig light chain polypeptides, and antibody conjugates, as well as methods of use of same.

The present invention relates to a method of providing thermal and/or acoustic insulation to a structure, comprising the steps of: providing a substrate which comprises fibres; applying the substrate to the structure; blending the substrate with a binder composition before, during or after application of the substrate to the structure; allowing curing of the binder composition after the substrate and the binder composition have been applied to the structure; wherein the binder composition comprises at least one hydrocolloid. The present invention also relates to an insulated structure obtainable by said method.

One or more embodiments of the present invention provide a microbial strain with improved productivity of ?-glutamylcysteine, bis-?-glutamylcystine, ?-glutamylcystine, reduced glutathione, and/or oxidized glutathione. Such microbial strain has disruption of [1] a gene encoding ?-glutamyltransferase and [2] a gene encoding phosphoglycerate mutase and enhanced expression of [3] a gene encoding glutamate-cysteine ligase and/or a gene encoding glutathione synthetase or [4] a gene encoding bifunctional glutathione synthetase. This invention also discloses a method for producing the substances mentioned above via culture of the microbial strain.

A fusion protein obtained by fusing a ferredoxin-thioredoxin reductase and thioredoxin via a linker peptide. The linker peptide includes glycine (G) and serine (S).

A process for the production of a target recombinant polypeptide is provided. The process comprises expressing an expression cassette encoding the target polypeptide and co-expressing an expression cassette encoding a mitochondrial foldase. Preferred mitochondrial foldases include Mia 40 and Erv1, and homologs thereof.

The present invention is an inducible coexpression system, capable of controlled induction of expression of each gene product.

A method of reducing an amount of a sulfur-containing compound in a reservoir fluid includes contacting a treatment fluid comprising an aqueous medium and an enzymatic scavenger with a precipitating fluid to precipitate the enzymatic scavenger; contacting the precipitated enzymatic scavenger with the reservoir fluid comprising the sulfur-containing compound; and reducing a number of the sulfur-containing compound in the reservoir fluid.

Provided is a method for the high expression of a recombinant human serum albumin, characterized in comprising the step of co-expressing: (a) a human serum albumin gene, and (b) one or more rHSA expression promoting factor genes in a yeast host cell.

The present invention relates to a polypeptide having glutathione reductase activity selected from the group consisting of: a) polypeptide having an amino acid sequence comprising the mature polypeptide sequence of SEQ ID NO: 1 or a 2) a polypeptide comprising an amino acid sequence that has at least 50% sequence identity with the mature polypeptide sequence of SEQ ID NO: 1.

The invention is based in part on the observation that a CHO cell oxidizing enzyme, particularly QSOX1, can survive a seemingly rigorous antibody purification process to reduce subsequent conjugation efficiency of the antibody to a drug. Whether the oxidizing enzyme survives the purification procedure depends on which purification techniques are employed which can vary from one antibody to another. With knowledge that contamination with a CHO cell oxidizing enzyme is a potential problem for subsequent conjugation, a suitable purification scheme can be devised for any antibody that eliminates or at least reduces CHO oxidizing enzyme(s) to an acceptable level.