Methods and compositions are described for management of the pharmacokinetic properties of active agents, e.g., therapeutic moieties, by conjugating, fusing, or non-direct linkage of the active agent to one or more wild-type or modified heparin-binding peptides (HB). Compounds may be administered to tissues including skin. Contemplated uses include treatment of disease, allergen immunotherapy, and immunization. Other aspects relate to compositions, methods and kits comprising heparin-binding peptides (HB) fused or conjugated to the therapeutic agents.

The present invention provides an anti-influenza virus agent that targets biomolecules of host cells including human cells and a method of screening a candidate molecule for the anti-influenza virus agent. That is, the present invention is an anti-influenza virus agent that has an effect of suppressing expression or a function of a gene that encodes a protein having an effect of suppressing incorporation of an influenza virus vRNA or an NP protein into influenza virus-like particles in host cells and the gene is at least one selected from the group including JAK1 gene and the like.

The present invention relates to the field of protein expression. More specifically, the present invention provides compositions and methods for increasing the expression and signaling of proteins on cell surfaces. In particular embodiments, the present invention provides nucleic acids and amino acid sequences useful for improving/increasing protein expression on the cell surface. In several embodiments, the sequences are operably linked to the N-terminal end of the protein of interest. The nucleic acid sequence encoding the sequence tag and the protein comprise part of an expression vector. The protein is expressed with the N-terminal sequence tag. In certain embodiments, the sequences of the present invention can be used with one or more chaperone or accessory proteins. In particular embodiments, the one or more chaperone/accessory proteins are encoded by the same vector or separate vectors. In other embodiments, the chaperone/accessory proteins are encoded the same vector that encodes the protein of interest.

This invention relates to LY6G6F, VSIG10, TMEM25 and LSR proteins, which are suitable targets for immunotherapy, treatment of cancer, infectious disorders, and/or immune related disorders, and drug development. This invention further relates to soluble LY6G6F, VSIG10, TMEM25 and LSR molecules, extracellular domains of LY6G6F, VSIG10, TMEM25 and LSR and conjugates, which are suitable drugs for immunotherapy, treatment of cancer, infectious disorders, and/or immune related disorders. This invention further relates to antibodies and antigen binding fragments and conjugates containing same, and/or alternative scaffolds, specific for LY6G6F, VSIG10, TMEM25 or LSR molecules, which are suitable drugs for immunotherapy, treatment of cancer, infectious disorders, and/or immune related disorders.

High affinity antibody antagonists of human interleukin-13 receptor alpha 1 are disclosed. The antibody molecules are effective in the inhibition of IL-13Rα1-mediated activities and, accordingly, present desirable antagonists for the use in the treatment of conditions associated with hIL-13Rα1 activity. The present invention also discloses nucleic acid encoding said antibody molecules, vectors, host cells, and compositions comprising the antibody molecules. Methods of using the antibody molecules for inhibiting or antagonizing IL-13Rα1-mediated activities are also disclosed.

Methods, devices, kits and systems for diagnosing inclusion body myositis (IBM) are provided. Methods, devices, kits and systems involves detecting the presence and/or level of autoantibodies that are reactive against at least a ˜43 kilodalton (kDa) protein or ˜43 kDa protein band from a muscle lysate or a mammalian cell lysate, or autoantibodies that are reactive against a cytosolic 5′-nucleotidase 1A protein (NT5C1A), or a cytosolic 5′-nucleotidase 1B protein (NT5C1B), or a NT5C1B isoform thereof, or a peptide fragment thereof, an isolated peptide thereof or a fusion protein comprising an isolated peptide of NT5C1A or NT5C1B. Such autoantibodies are only found in IBM patients and not in patients with other myopathies.

The present application belongs to the field of functional peptides and more particularly to the field of controlled protein aggregation. The invention discloses molecules of a peptide structure as defined in the claims and methods of using such molecules for therapeutic applications and for diagnostic uses, as well as in other applications such as in the agbio field and in industrial biotechnology. The molecules can be used for curing and/or stabilizing infections such as bacterial,fimgal and viral diseases, but are also useful in non-infectious human and veterinary diseases. The molecules can also be used for the detection of protein biomarkers and for the prognosis and diagnosis of a variety of diseases.

Methods for enhancing cellular uptake of cargo molecules by boronating the cargo molecule, particularly with one or more phenylboronic acid groups. Boronation reagents for reversible boronation of cargo molecules, particularly, cargo molecules having one or more amino groups are provided.

Methods and compositions related to a nucleic acid-guided nuclease cell targeting screen are provided. The invention relates to compositions and methods for identifying cell targeting proteins that, when associated with a nucleic acid-guided nuclease (such as Cas9), enables at least the nucleic acid-guided nuclease to be targeted to the surface of a target cell or internalized by a target cell, i.e., a cell targeted by the cell targeting agent.

GPCR-fusion partner proteins comprising G protein coupled receptors (GPCRs) of GPCRs and fusion partners such as rubredoxin, cytochrome b562 RIL (Bril, bRIL, BRIL), T4 lysozyme C-terminal fragment (C-term-T4L), flavodoxin, or xylanase either substituted for some or all of the third intracellular loop of the GPCR between the fifth and sixth helix of the GPCR are described or attached to an terminus or C terminus of the GPCR. GPCR-fusion partner proteins in crystalline form, optionally of a quality suitable for x-ray crystallographic structure determination of the GPCR, are described. Methods of using fusion partners in GPCR-fusion partner proteins to support crystallization of GPCR-fusion partner proteins for x-ray crystallographic structure determination of the GPCR, are described. Methods of identifying other suitable fusion partners through screening of protein data banks are also described.