The present disclosure provides a heterodimeric, conditionally active chimeric antigen receptor (CAR), and a nucleic acid comprising a nucleotide sequence encoding the CAR. The present disclosure provides cells genetically modified to produce the CAR. A CAR of the present disclosure can be used in various methods, which are also provided.

This application relates to anti-D-Dimer recombinant antibodies that specifically bind to fibrin and fibrinogen degradation products (FDP) such as D-Dimer, fragment DD and fragment D with high binding affinity and do not bind to fragment E and fibrinogen. The present invention also refers to methods and assays for detection of D-Dimer and FDP fragments in samples using said recombinant antibodies.

The present disclosure is directed to a system for displaying antigens. This system includes an outer membrane vesicle comprising a lipid bilayer and a synthetic antigen receptor comprising an outer membrane scaffold protein fused to a biotin-binding protein, where the outer membrane scaffold protein is incorporated in the lipid bilayer and the biotin-binding protein is displayed outside the outer membrane vesicle. Also disclosed are therapeutic compositions, nucleic acid constructs, expression vectors, and methods of eliciting an immune response in a subject.

Described herein is a bifunctional peptide, compositions comprising the same, and methods useful for treatment of peri-implant disease.

The present invention relates to a novel method for the affinity purification of proteins of interest in a single step, based on the lectin activity of the CRD (Carbohydrate Recognition Domain) of a galectin or part of said domain retaining the ability to bind β-galactosidase derivative.

Some aspects of this disclosure provide a fusion protein comprising a guide nucleotide sequence-programmable DNA binding protein domain (e.g., a nuclease-inactive variant of Cas9 such as dCas9), an optional linker, and a recombinase catalytic domain (e.g., a tyrosine recombinase catalytic domain or a serine recombinase catalytic domain such as a Gin recombinase catalytic domain). This fusion protein can recombine DNA sites containing a minimal recombinase core site flanked by guide RNA-specified sequences. The instant disclosure represents a step toward programmable, scarless genome editing in unmodified cells that is independent of endogenous cellular machinery or cell state.

The present invention relates, in part, to chimeric proteins that find use in various immunotherapies. Particularly, the present invention provides targeted therapeutic agents that modulate the immune system for the treatment of diseases such as cancer.

The technology described herein is directed to regulated synthetic gene expression systems. In one aspect described herein are synthetic transcription factors (synTFs) comprising a DNA binding domain, a transcriptional effector domain, and a regulator protein. In other aspects described herein are gene expression systems comprising said synTFs and methods of treating diseases and disorders using said synTFs.

The present disclosure a cohort of sialic acid binding molecules which comprise one or more modified carbohydrate binding modules (CBMs). The modified CBMs reduce the risk of adverse events related to the host immune response and/or the production of anti-drug antibodies (ADAs). The modified CBMs can be used in therapy or as medicaments and find specific application as molecules for the modulation of an immune response and/or cell growth. The modified CBMs may also be used as adjuvants, for example mucosal adjuvants and in the treatment and/or prevention of cancer, sepsis and/or diseases caused or contributed to by a pathogen that binds cell surface sialic acid-containing receptors.

The present invention relates to polypeptides comprising comprising a first chain comprising an amino acid sequence having at least 80% sequence identity to SEQ ID NO:1; a second chain comprising an amino acid sequence having at least 80% sequence identity to SEQ ID NO:2; and a linker linking the first and second chain. In addition, the present invention is directed to methods of using these polypeptides as calibrators and standards in diagnostic methods.