Provided is a composition by which glycated hemoglobin can be measured even in the presence of a stronger surfactant than a conventional case. Also provided is a buffer and/or stabilizer which maintains the residual activity of an amadoriase or lowers a reduction of residual activity. The present invention provides a composition for use in measuring glycated hemoglobin containing an amadoriase having substitution of one or more amino acid residues at a position(s) corresponding to an amino acid(s) selected from the group consisting of position 262, position 257, position 249, position 253, position 337, position 340, position 232, position 129, position 132, position 133, position 44, position 256, position 231 and position 81 of an amadoriase derived from the genus Coniochaeta and represented by SEQ ID No: 1 or 3, and having residual activity even in the presence of a surfactant. The present invention also provides a composition and kit for use in measuring glycated hemoglobin, comprising a specific stabilizer and/or a buffer. The present invention can provide an enzyme and a composition for use in measuring glycated hemoglobin, excellent in storage stability even if they are exposed to a surfactant.

The present specification discloses a urate oxidase-albumin conjugate, a preparation method thereof, a urate oxidase variant contained in the urate oxidase-albumin conjugate, and a preparation method thereof. The urate oxidase-albumin conjugate is characterized in that three or more albumins are conjugated to the urate oxidase variant through a linker, thereby improving half-life and reducing immunogenicity. In addition, the urate oxidase-albumin conjugate can be used to prevent or treat various diseases, disorders and/or indications caused by uric acid.

A genetically engineered bacterium includes a genome of the Eschericia coli and a mutant encoding gene hisG* of a Corynebacterium glutamicum ATP phosphoribosyl transferase HisG on the genome, and the gene hisG* is strongly expressed to enhance activity of a key enzyme HisG for histidine synthesis. The gene hisG* has a nucleotide sequence as shown in SEQ ID NO: 1; a copy number of histidine operon genes hisDBCHAFI of the Eschericia coli is further increased on the genome to enhance a terminal synthetic route of histidine; an encoding gene lysE from an arginine/lysine transportprotein of the Corynebacterium glutamicum is further integrated to the genome and strongly expressed to promote the intracellular histidine secrete to the extracellular space; and an encoding gene rocG of glutamate dehydrogenase of Bacillus subtilis is further integrated to the genome and strongly expressed to promote generation of histidine.

The present disclosure provides a genetically modified mouse comprising a genomic nucleic acid encoding human APOE4, a genomic nucleic acid encoding mouse TREM2 modified to include a R47H substitution, and at least one genomic modification selected from the group consisting of: (a) a genomic nucleic acid encoding mouse ABCA7 modified to include an A 1541 G substitution; (b) a genomic nucleic acid encoding mouse APP modified to include G60IR, F606Y, and R609H substitutions; (c) a genomic nucleic acid encoding mouse PLCG2 modified to include a M28L substitution; (d) a genomic nucleic acid encoding mouse MTHFR modified to include a A262V substitution; (e) an inactivated Ceacaml allele; and (f) an inactivated II1rap allele. Methods of producing the genetically modified mouse and methods of using the genetically modified mouse are also provided.

A mutant glycine oxidase is obtained by substituting at least one wild-type amino acid sequence derived from thermophilic bacteria belonging to the family Bacillus with another amino acid, and has the following enzyme properties. Molecular weight: 40,000±2,000 daltons by SDS-PAGE. Optimum temperature: 45° C. under the condition of pH 8.5 in presence of pyrophosphate. Optimum pH: pH 8.0 under the condition of 37° C. in presence of pyrophosphate. Thermal stability: Stable up to 70° C. under the condition of pH 8.5 while retaining for 1 hour in presence of pyrophosphate. pH Stability: Stable in the range of pH 5.5 to 10.0 under the condition of 4° C. while retaining for 24 hours in presence of pyrophosphate. Specific activity: 1.2 units/mg or more. Kinetic constant K.sub.m: 0.2 mM or less.

Provided herein is a non-naturally occurring microbial organism (NNOMO) having a methanol metabolic pathway (MMP) that can enhance the availability of reducing equivalents in the presence of methanol. Such reducing equivalents can be used to increase the product yield of organic compounds produced by the microbial organism, such as succinate. Also provided herein are methods for using such an organism to produce succinate.

A method for the bio-production of threonine including genetically modified yeasts and a method in which they are used to produce threonine, as compared to the parent yeasts.

A genetically engineered bacterium includes a genome of the Eschericia coli and a mutant encoding gene hisG* of a Corynebacterium glutamicum ATP phosphoribosyl transferase HisG on the genome, and the gene hisG* is strongly expressed to enhance activity of a key enzyme HisG for histidine synthesis. The gene hisG* has a nucleotide sequence as shown in SEQ ID NO: 1; a copy number of histidine operon genes hisDBCHAFI of the Eschericia coli is further increased on the genome to enhance a terminal synthetic route of histidine; an encoding gene lysE from an arginine/lysine transportprotein of the Corynebacterium glutamicum is further integrated to the genome and strongly expressed to promote the intracellular histidine secrete to the extracellular space; and an encoding gene rocG of glutamate dehydrogenase of Bacillus subtilis is further integrated to the genome and strongly expressed to promote generation of histidine.

The present disclosure relates to compositions and methods for using cells having chemically-induced fusion protein complexes to spatially and temporally control immune cell signal initiation and downstream responses for treating disease. As a preferred example, the present disclosure relates to fusion polypeptides comprising (a) a first polypeptide comprising a first secretion signal, a first multimerization domain, a first transmembrane domain, and an actuator domain, (b) a viral self-cleaving polypeptide, and (c) a second polypeptide comprising a second secretion signal, a binding domain that comprises a single chain antibody, a receptor ectodomain, or a ligand, a second multimerization domain, and a second transmembrane domain.

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as α-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ε-Caprolactone, 6-amino-hexanoic acid, ε-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear α-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 β-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 β-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.