G01N2333/988

Modified biosensors and biocatalysts and methods of use

Biosensors including a nucleic acid encoding a PcaU protein, a PobR protein, a CatM protein, a PcaR protein, or a TphR protein are provided. In some examples, the biosensors include a promoter regulated by the sensed molecule operably linked to a reporter gene. The biosensors may be included in a vector or in cells including one or more of the biosensors or vectors. Modified chorismate pyruvate lyase (UbiC) and modified paraoxonase (PON1) proteins including one or more amino acid substitutions are provided. Finally, methods of selecting biocatalysts with increased activity including transforming a library of cells expressing a biosensor with one or more nucleic acids encoding one or more mutations in a gene involved in a biosynthesis pathway, determining activity of the reporter protein; and selecting a cell with increased reporter protein activity as expressing a biocatalyst with increased activity are provided.

CRYSTALLIZED OXALATE DECARBOXYLASE AND METHODS OF USE

Oxalate decarboxylase crystals, including stabilized crystals, such as cross-linked crystals of oxalate decarboxylase, are disclosed. Methods to treat a disorder associated with elevated oxalate concentration using oxalate decarboxylase crystals are also disclosed. Additionally disclosed are methods of producing protein crystals.

METHODS TO DETERMINE WHETHER A SUBJECT IS SUITABLE OF BEING TREATED WITH AN AGONIST OF SOLUBLE GYANYLYL CYCLASE (SGC)

The present invention provides a method for determining whether a human or animal subject suffers from oxidative stress, is suitable of being treated with an antioxidant and/or free radical scavenger, and/or is suitable of being treated with an agonist of soluble Guanylyl Cyclase (sGC), in particular with an activator of sGC, said method comprising the steps of providing a tissue or liquid sample from said subject, and determining whether or not said sample is characterized by the presence, upregulation or overexpression of sGC comprising a heme free β1 subunit.

TREATMENT STRATIFICATION FOR AN EXACERBATION OF INFLAMMATION
20220120760 · 2022-04-21 ·

Provided are methods of analysing markers of eosinophil levels and/or markers of neutrophil levels in a blood sample from a patient suffering from an exacerbation of inflammation of a respiratory condition to determine the levels of eosinophils and/or neutrophils respectively. The methods may involve selecting an appropriate treatment. Systems and kits for performing the analysis are also provided.

Mutated histidine decarboxylase and use thereof

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.

Enolase 1 (ENO1) compositions and uses thereof

The invention provides compositions comprising Eno1 for delivery to a muscle. Further, the invention provides a method for normalizing blood glucose in a subject with elevated blood glucose, comprising administering to the subject enolase 1 (Eno1), thereby normalizing blood glucose in the subject. The invention also provides methods of treating one or more conditions including impaired glucose tolerance, insulin resistance, pre-diabetes, and diabetes, especially type 2 diabetes in a subject, comprising administering to the subject enolase 1 (Eno1), thereby treating the condition in the subject. In certain methods of the invention, the Eno1 is delivered to muscle.

Methods Employing Mucin-Specific Proteases

The present disclosure provides compositions and methods involving the use of mucin-specific proteases for mucin-specific cleavage, labeling, and/or enrichment of mucin domain glycoproteins. Also provided are methods for the analysis of mucin-domain glycoproteins useful in glycomapping of mucin glycosites and their associated glycoforms. Provided compositions and methods are also useful for selective cleavage, release, and enrichment of mucins from cell and tissue samples, for the study of native mucin biology, and for the detection and analysis of mucins that are aberrantly expressed in various conditions, including cancer.

CARBONIC ANHYDRASE TARGETING AGENTS AND METHODS OF USING SAME
20220023277 · 2022-01-27 ·

The invention provides agents that target carbonic anhydrase, which can be used as imaging agents or therapeutic agents. The agents can be used to image tumor hypoxia as well as other physiological processes in a subject.

CA IX - NIR DYES AND THEIR USES
20230320564 · 2023-10-12 ·

The present disclosure relates to compounds that are useful as near-infrared fluorescence probes, wherein the compounds include i) a ligand that binds to the active site of carbonic anhydrase, ii) a dye molecule, and iii) a linker molecule that comprises an amino acid, amide, ureido, or polyethylene glycol derivative thereof. The disclosure further describes methods and compositions for making and using the compounds, methods incorporating the compounds, and kits incorporating the compounds.

MUTATED HISTIDINE DECARBOXYLASE AND USE THEREOF

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.