Improved formulations of lipid nanoparticles are provided. Use of the lipid nanoparticles for delivery of a therapeutic agent and methods for their preparation are also provided.

Disclosed herein are means for the detection and characterization of neurotoxins such as botulinum neurotoxin (BoNT) or tetanus neurotoxin. The present disclosure provides methods for determining potency and activity of neurotoxins in vitro and in vivo. Also disclosed are polypeptides comprising N- and C-terminal fragments of a reporter protein that are split by a linker comprising a neurotoxin cleavage site. Cleavage of the linker by a neurotoxin decreases reporter protein activity, thereby indicating activity of the neurotoxin. Compositions and kits comprising the disclosed polypeptides, nucleic acids comprising nucleotide sequences encoding such polypeptides, and cells expressing such polypeptides are also disclosed.

A new thermostable luciferase of the following mutant luciferase (a) or (b): (a) a mutant of a wild-type luciferase comprising the amino acid sequence of SEQ ID NO: 1, wherein phenylalanine at position 292 and/or phenylalanine at position 294 in the amino acid sequence of SEQ ID NO: 1 is substituted with another amino acid; or (b) a mutant of a luciferase having 93% or more homology with the amino acid sequence of SEQ ID NO: 1, wherein in the amino acid sequence of the mutant, the amino acid at a site corresponding to position 292 and/or position 294 in the amino acid sequence of SEQ ID NO: 1 is substituted with another amino acid.

Provided are nucleic acids that include a promoter, where the promoter is operable in a Bacteroides cell and is operably linked to a heterologous nucleotide sequence of interest. Also provided are nucleic acids that include a promoter (operable in a prokaryotic cell such as a Bacteroides cell) operably linked to a sequence encoding a synthetic ribosomal binding site (RBS). Also provided are fusion proteins (and nucleic acids encoding them) in which a secreted Bacteroides polypeptide is fused to a heterologous polypeptide of interest. Also provided are prokaryotic cells (e.g., E. coli, a Bacteroides cell, and the like) that include one more nucleic acids such as those described above. Also provided are methods of expression in a prokaryotic cell, methods of detectably labeling a Bacteroides cell in an animal's gut, and methods of delivering a protein to an individual's gut.

Provided herein are enhanced luciferase enzymes for use with thermostable luciferin analogs for bioluminescent assays. In particular, the present disclosure provides compositions, assays, and methods for performing a bioluminescent assay using enhanced, high-activity luciferase enzymes compatible with thermostable luciferins, such as 5,5-disubstituted luciferin analogs.

Polypeptide are disclosed that comprise an amino acid sequence at least 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the amino acid sequence selected from the group consisting of SEQ ID NO:1-1615, not including any functional domains added fused to the protein (whether N-terminal, C-terminal, or internal), and wherein the 1, 2, 3, 4, or 5 N-terminal and/or C-terminal amino acid residues may be present or absent when considering the percent identity.

A functional cell-based assay for use as a bioidentity assay for insulin or insulin analogs is described. The assay may be used as a replacement of the rabbit blood sugar method disclosed in USP<121> Insulin Assays.

The present invention refers to a method for controlling undesired vegetation at a plant cultivation site, the method comprising the steps of providing, at said site, a plant that comprises at least one nucleic acid comprising a nucleotide sequence encoding a wild-type hydroxyphenyl pyruvate dioxygenase or a mutated hydroxyphenyl pyruvate dioxygenase (mut-HPPD) which is resistant or tolerant to a HPPD-inhibiting herbicide and/or a nucleotide sequence encoding a wild-type homogentisate solanesyl transferase or a mutated homogentisate solanesyl transferase (mut-HST) which is resistant or tolerant to a HPPD-inhibiting herbicide, applying to said site an effective amount of said herbicide. The invention further refers to plants comprising mut-HPPD, and methods of obtaining such plants.

The present invention provides a lipoxygenase that enables the highly efficient formation of an oxide of a highly unsaturated fatty acid or an oxide of a highly unsaturated fatty acid derivative from a highly unsaturated fatty acid or a highly unsaturated fatty acid derivative. The present invention provides a lipoxygenase that enables the highly efficient formation of 8-hydroxyeicosatetraenoic acid from arachidonic acid, the highly efficient formation of 8-hydroxyeicosapentaenoic acid from eicosapentaenoic acid, and the highly efficient formation of 10-hydroxy docosahexaenoic acid from docosahexaenoic acid. Specifically, the present invention provides a polynucleotide that comprises the nucleic acid sequence represented by SEQ ID NO: 1 and 3, or a homolog thereof, and a polypeptide that comprises the amino acid sequence represented by SEQ ID NO: 2 and 4, or a homolog thereof. Also provided is a composition that comprises a membrane protein of an organism belonging to the class Malacostraca and is for carrying out a lipoxygenase reaction.

The present disclosure relates to a recombinant protein comprising a plurality of type II cohesin repeats. The present disclosure provides a recombinant cellulosome complex comprising: the recombinant protein comprising a plurality of type II cohesin repeats; a recombinant cellulosome complex integrating protein A comprising a plurality of type I cohesin repeats, a plurality of cellulose-binding modules and a type II dockerin; and a plurality of recombinant enzymes each comprising a type I dockerin. A cell, a method for digesting a cellulose and a method for producing ethanol are also provided.