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.

Provided herein are inhibitor-resistant luciferase mutants, and methods of use thereof. In particular, luciferase mutants are provided that are thermal stable and exhibit improved stability in the presence of luciferin break-down products, such as dehydroluciferin. Further provided are assay systems comprising inhibitor-resistant luciferase mutants and amino acid sequences of the inhibitor-resistant luciferase mutants.

The present invention relates to methods and compositions that include enzymes and/or binding polypeptides useful for protecting polymers from damage caused by fatty acids from secreted biological fluids such as sebum or sweat.

Provided herein are compositions and methods for the assembly of a bioluminescent complex from two or more non-luminescent (e.g., substantially non-luminescent) peptide and/or polypeptide units. In particular, bioluminescent activity is conferred upon a non-luminescent polypeptide via structural complementation with another, complementary non-luminescent peptide.

A barley plant including a mutant LOX-1 protein and that is deficient in lipoxygenase activity.

The present disclosure relates, in general, to a fusion protein construct comprising RNase L and a split reporter system, and methods of using the reporter for detecting 2′-5′ linked oligoadenylates (2-5A) and double stranded RNA in vivo.

Disclosed is a method for purifying a protein, comprising steps of: preparing a sample containing a fusion protein containing an amino acid sequence of a peptide tag and an amino acid sequence of a target protein; and separating contaminant proteins contained with the fusion protein in the sample and the fusion protein in the sample, wherein the peptide tag contains 12 or more acidic amino acid residues.

The present invention describes an alternative approach to increase Taurine (Tau) or methionine (Met) production in eukaryotes, namely by the insertion of components of a sulfur-metabolic pathway and Tau- or Met-binding proteins in organisms where the peptides do not exist or have not clearly been identified. The invention describes methods for the use of polynucleotides that encode functional cysteine dioxygenase (CDO) alone, sulfinoalanine decarboxylase (SAD) alone or CDO and SAD polypeptides in combination with functional Tau- or Met-binding proteins in plants to increase Tau or Met production. The preferred embodiment of the invention is in plants but other organisms may be used. Increased Tau or Met availability will improve nutritional value of the crop.

Disclosed are methods of determining activity of CDK4 and CDK6 variants upon exposure to CDK inhibitors, methods for determining activity of a Rb variant, methods for determining the activity of a p16 variant in a cell, and methods for determining the sensitivity of a CDK4 variant or a CDK6 variant to p16 in a cell. Stable cell lines for determining activity of CDK4 variants, CDK6 variants, Rb variants, and p16 variants are also disclosed.

The present invention relates to the development of genetically engineered yeasts that can produce hydrocarbons in a controllable and economic fashion. More specifically the invention relates to the production of liquid alkanes and alkenes that can be used for liquid transportation fuels, specialty chemicals, or feed stock for further chemical conversion.