The present disclosure provides anti-SAS1B antibodies, antigen-binding fragments thereof, and antibody-drug conjugates and methods of their use. This present disclosure also provides an isolated antibody or antigen-binding portion thereof having at least one of SB antibodies binding to surface exposed SAS1B, and 6B1 antibodies identifying at least one set of cancer patients testing positive for SAS1B expression.

The invention relates to recombinant nucleic acid and polypeptides encoding collagenase I and collagenase II, methods for the preparation thereof and methods for the use thereof. The invention also encompasses methods related to releasing a composition comprising collagenase prior to therapeutic administration.

Compositions and methods are provided that reduce the time required for detection of botulinum neurotoxins in cell-based assays. In one aspect an isoquinolynyl compound can be used for this purpose. In such cell-based assays the cell can include an enzyme that facilitates degradation of the reporter significantly faster after the cleavage than before the cleavage, and presence of the Botulinum toxin correlates with reduction of the signal from a baseline signal. The cell can advantageously express both the construct that includes the reporter, and an enzyme that facilitates the degradation.

Methods for quantifying the amount of drug present in a prodrug composition are provided.

The present disclosure relates to methods and compositions for detecting mitochondrial dysfunction. In particular, the disclosure relates to reporter molecules that are cleavable by the zinc metalloprotease Metalloendopeptidase OMA1 (OMA1). In each embodiment, the reporter molecules of the invention are particularly useful for drug discovery and detection of diseases associated with mitochondrial dysfunction.

The invention relates to recombinant nucleic acid and polypeptides encoding collagenase I and collagenase II, methods for the preparation thereof and methods for the use thereof. The invention also encompasses methods related to releasing a composition comprising collagenase prior to therapeutic administration.

Aspects of the present disclosure relate to methods and compositions useful for in vivo and/or in vitro profiling of environmental triggers (e.g., enzyme activity, pH or temperature). In some embodiments, the disclosure provides methods of in vivo enzymatic processing of exogenous molecules followed by detection of nanocatalysts as representative of the presence of active enzymes (e.g., proteases) associated with a disease, for example, cancer or infection. In some embodiments, the disclosure provides compositions and methods for production of in vivo sensors comprising nanocatalysts.

A method of predicting if a subject has an Activated B Cell-like (ABC) subtype or a non-ABC subtype of Diffuse Large B-Cell Lymphoma (DLBCL), comprising (a) obtaining a sample from the subject; (b) measuring the expression levels of CD10, MUM1, FOXP1, and optionally Bcl-6; (c) determining a composite score based on the expression levels of CD10, MUM1, and FOXP1, and optionally Bcl-6; and (d) predicting if the subject has an ABC subtype or a non-ABC subtype of DLBCL based on the composite score.

The invention relates to recombinant nucleic acid and polypeptides encoding collagenase I and collagenase II, methods for the preparation thereof and methods for the use thereof. The invention also encompasses methods related to releasing a composition comprising collagenase prior to therapeutic administration.

An unprecedented mechanism of ubiquitination that is independent of E1 and E2 enzymes, instead relying on activation of ubiquitin by ADP-ribosylation, and which is mediated by members of the SidE effector family encoded by the bacterial pathogen Legionella pneumophila is disclosed. The herein disclosed method demonstrates a method in which ubiquitination can be carried out by a single enzyme. In addition, the present disclosure also provides compositions that may be used in ubiquitination assays and/or methods of screening active substance that may inhibit the ubiquitination process.