The present invention relates to a fusion protein for enhancing expression efficiency of a target protein. More specifically, the present invention relates to a glutamyl-prolyl-tRNA synthetase from human (hEPRS) WHEP domain (including WHEP domains TRS-1, TRS-2, and TRS-3 which locate at middle sites of the EPRS protein, and linkers connecting the three domains therethrough). When used as a fusion protein for expressing a target protein in E. coli, the hEPRS WHEP domain according to the present invention enhanced water solubility of the target protein.

The present invention relates to a novel peptide or a partial sequence thereof for enhancing expression efficiency of a target protein, and a fusion protein comprising the same. The novel peptide according to the present invention can enhance expression efficiency of a target protein, and furthermore, the peptide can also be applied to a solubility-enhancing fusion protein in order to enhance solubility of the target protein, so that solubility as well as expression efficiency of the target protein is enhanced, which allows such a peptide to be usefully used for production of a recombinant target protein.

The present invention provides DNA vaccines for the treatment of allergies. The vaccines comprise the coding sequence for one or more allergenic epitopes, and preferably the full protein sequence, of the allergenic protein from which the epitope(s) is derived, fused inframe with the lumenal domain of the lysosomal associated membrane protein (LAMP) and the targeting sequence of LAMP. The vaccines allow for presentation of properly configured three dimensional epitopes for production of an immune response. The vaccines can be multivalent molecules, and/or can be provided as part of a multivalent vaccine containing two or more DNA constructs.

A novel class of fusion proteins to recruit a cell's innate chaperone mechanism, specifically the Hsp70-mediated system, to specifically reduce α-synuclein-mediated protein aggregation and associated proteopathies is disclosed.

The invention relates to an N-terminal extension sequences which are employed to enhance the expression of recombinant therapeutic peptides. The invention also relates to a process for the high-level expression of recombinant therapeutic peptides using the said N-terminal extension sequence. The invention also provides nucleic acids, vectors and recombinant host cells for efficient production of biologically active proteins such as lirapeptide.

The invention concerns soluble and antigenic HTLV p24 variants that can be fused to chaperones and their use in diagnostic applications such as immunoassays for detecting antibodies against HTLV-I or HTLV-II in an isolated biological sample. In particular, the invention relates to a soluble HTLV-I or HTLV-II p24 antigen comprising either the N- or the C-terminal domain of p24 and lacking the other domain. Moreover, the invention covers recombinant DNA molecules encoding these HTLV-I and -II fusion antigens as well as their recombinant production using expression vectors and host cells transformed with such expression vectors. In addition, the invention focuses on compositions of these HTLV p24 antigens with HTLV gp21 antigen and on an immunoassay method for detection of HTLV antibodies using the antigens of the invention. Also the use of HTLV p24 antigens in an in vitro diagnostic assay as well as a reagent kit for detection of anti-HTLV-antibodies comprising said HTLV antigens is encompassed.

Provided is a polypeptide tag. The amino acid sequence of the polypeptide tag is Xaa1Xaa2Xaa3PHDYNXaa4Xaa5Xaa6 (SEQ ID NO: 37), wherein in the formula, Xaa1, Xaa2, Xaa3, Xaa4, Xaa5, and Xaa6 are each independently an amino acid or none. The polypeptide tag is used for labeling a target protein. In a second aspect, provided is a polypeptide fusion protein, comprising the following two structures: (1) any polypeptide tag according to the first aspect, and (2) a target protein connected to the polypeptide tag. Also provided are an in vitro cell-free protein synthesis system and an application thereof in in vitro protein synthesis. By constructing the polypeptide tag and a target protein as a fusion protein, the expression of the labeled target protein can be effectively increased without removing the polypeptide tag.

Disclosed are a thioredoxin mutant, preparation method thereof, and application thereof in production of recombinant fusion protein. The recombinant fusion protein produced by the expression of the thioredoxin mutant of the present invention has good solubility and stability in high-temperature environments and is not easily denatured.

The present invention relates, in part, to pegylated chimeric proteins comprising one or more targeting moieties, linkers, and one or more signaling moieties, or variants thereof, and their use as therapeutic agents.

The present invention relates to human IgG Fc domain variants with improved effector function and uses thereof.