The present invention relates to a new isolated polypeptide comprising an amino acid sequence having at least 94%, 95%, 99% or 100% identity to the full length amino acid sequence set forth in SEQ ID NO: 1, and having a polyester degrading activity, and uses thereof.

The present invention relates to methods of treating a disease, and methods for reduction of the formation of anti-drug antibodies (ADAs) in response to the administration of a therapeutic agent. The invention further relates to methods of treating a disease, particularly a B-cell proliferative disorder, and methods for reduction of adverse effects in response to the administration of a therapeutic agent, particularly a T-cell activating therapeutic agent.

Provided are a TEV protease variant, a fusion protein thereof, a preparation method therefor and the use thereof. Provided are a TEV protease variant with unique properties obtained by screening and a fusion protein thereof. The TEV protease variant has a low enzyme cleavage activity during expression in hosts, and preferably has a lower enzyme cleavage activity compared to an S219V variant having an amino acid sequence as shown in SEQ ID NO: 10. The enzyme cleavage site of the TEV protease variant is selected from EXXYXQG/S/H, wherein X is any amino acid residue, and the enzyme cleavage site is preferably selected from SEQ ID NO: 7 and 8. Fusion expression using the TEV protease variant of the present invention and a polypeptide can be used for preparing a polypeptide quickly and efficiently, thereby solving the problems currently present in the process of the recombinant production of a polypeptide.

Expression vectors and methods of protein purification, which allow for selection of full length protein over truncated forms of the protein being purified, are disclosed. The methods express a target protein as a three domain fusion, represented by formula I: A-[L.sub.1]-B-[L.sub.2]-C, where A is a first purification tag domain, C is the second purification tag domain and B is the target protein domain. A, B and C are preferably covalently linked by linkers, L.sub.1 and L.sub.2 as shown in Formula I, however, L.sub.1 and L.sub.2 may be optional. The purification tags at the N and C termini are different.

Expression vectors including nucleic acid sequences which encode the fusion protein represented by formula I are also disclosed. The vectors are used with host expression systems such as insect, yeast, or mammalian cells to express the target protein, which is subsequently purified as a function of the different affinity tags.

A method for producing a nuclease of a gram negative bacterium or a nuclease preparation containing a nuclease of a gram negative bacterium including expression of the nuclease in a gram positive bacterium and subsequent secretion of the nuclease, as well as a nuclease or a nuclease preparation that can be obtained by this method.

Provided herein, among other things, is a conjugate comprising a polymerase and a nucleoside triphosphate, where the polymerase and the nucleoside triphosphate are covalently linked via a linker that comprises a cleavable linkage. A set of such conjugates, where the conjugates correspond to G, A, T (or U) and C is also provided. Methods for synthesizing a nucleic acid of a defined sequence are also provided. The conjugates can also be used for sequencing applications.

The present disclosure provides, inter alia, genetically encoded recombinant peptide biosensors comprising analyte-binding framework portions and signaling portions, wherein the signaling portions are present within the framework portions at sites or amino acid positions that undergo a conformational change upon interaction of the framework portion with an analyte.

An isolated nucleic acid that includes an open reading frame encoding a lanthipeptide protease polypeptide for scarless tag removal from a polypeptide is presented. Reagents, expression constructs and methods are also provided for preparing a scarless tag polypeptide product from a tagged polypeptide precursor containing a lanthipeptide protease cleavage site. The reagents are directed to novel lanthipeptide proteases and expression constructs and polypeptide precursors that include highly specific lanthipeptide protease substrate recognition sequence. Methods are provided that enable scarless tag removal from a cognate lanthipeptide, a non-cognate lanthipeptide or a heterologous polypeptide that includes extraneous amino acid sequences, such as leader peptides and tags.

The disclosure provides for screening methodologies using gene fragment overexpression that provide for the identification of peptide sequences which can modulate the functional regions of proteins of interests, and uses thereof. The disclosure further relates to peptide, polypeptide and polynucleotide identified by the methods of the disclosure, compositions containing such peptide, polypeptide and polynucleotides and uses thereof.

Provided are a baicalein- and scutellarein-synthesizing microorganism, a preparation method for same, and applications thereof. By modifying a heterologous metabolic pathway of a host cell per a genetic engineering method, acquired is an engineered strain providing a high yield of baicalein and scutellarein. Also provided is a process for utilizing the engineered strain to produce baicalein and scutellarein.