The present invention relates to a fusion protein comprising an endolysin with an amino acid sequence according to SEQ ID NO: 1 and fragments and/or derivatives thereof and an additional cationic or polycationic peptide, an amphipatic peptide, a sushi peptide, a defensin, a hydrophobic peptide or an antimicrobial peptide fused to said endolysin, fragment and/or derivative at the N- and/or C-terminus. Moreover, the present invention relates to nucleic acid molecules encoding said fusion protein, vectors comprising said nucleic acid molecules and host cells comprising either said nucleic acid molecules or said vectors. In addition, the present invention relates to said fusion protein for use as a medicament, in particular for the treatment or prevention of staphylococcal infections, as diagnostic means, as cosmetic substance or as sanitizing agent. The present invention also relates to the use of said fusion protein for the treatment or prevention of staphylococcal contamination of foodstuff, of food processing equipment, of food processing plants, of feed for livestock animals, of surfaces coming into contact with foodstuff, of medical devices, of surfaces in hospitals and surgeries. Furthermore, the present invention relates to a pharmaceutical composition comprising said fusion protein.

The present invention relates to the purification of target molecules like recombinant and/or biotherapeutic proteins. Activated carbon can be used to remove leachables and/or extractables resulting from disposable equipment employed in the process.

The present invention relates to the purification of target molecules like recombinant and/or biotherapeutic proteins. Activated carbon can be used to remove leachables and/or extractables resulting from disposable equipment employed in the process.

Specific peptides, and derived ionization characteristics of the peptides, from the Fatty acid synthase (FASN) protein are provided that are particularly advantageous for quantifying the FASN protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the FASN protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an FASN peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.

The present disclosure provides conditionally active, heterodimeric polypeptides. The conditionally active, heterodimeric polypeptides are active in the presence of a dimerizing agent that induces dimerization of the polypeptides of the heterodimer. A conditionally active, heterodimeric polypeptide of the present disclosure is useful in a variety of research and treatment methods, which are also provided.

The present disclosure provides conditionally active, heterodimeric polypeptides. The conditionally active, heterodimeric polypeptides are active in the presence of a dimerizing agent that induces dimerization of the polypeptides of the heterodimer. A conditionally active, heterodimeric polypeptide of the present disclosure is useful in a variety of research and treatment methods, which are also provided.

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.

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.

The present invention discloses a method for preparing glatiramer acetate, comprising: (1) dissolving L-alanine NCA, L-tyrosine NCA, L-glutamic acid-γ-benzyl ester NCA, and L-ε-trifluoroacetyl-lysine NCA in 1,4-dioxane as solvent, stirring until a clarified solution is formed; (2) adding diethylamine for catalysis, stirring at 20-25° C., then slowly pouring the reaction solution into water, collecting the produced white product; (3) adding the obtained product to a solution of hydrobromic acid in acetic acid, stirring at 23.0-25.0° C., pouring the reaction solution into purified water for quenching and stirring, subjecting the mixture to suction filtration to obtain a yellow solid, after repeating 3-5 times, subjecting the solid to blast drying to remove the moisture therein; and (4) dissolving the solid obtained in step (3) in a 1M piperidine aqueous solution at room temperature and stirring, subjecting the obtained solution to dialysis, adding glacial acetic acid to adjust the pH to 5.5-7.0, and lyophilizing.

The present invention relates to fluorescent dyes. The present invention provides a wide range of fluorescent dyes and kits containing the same, which are applicable for labeling a variety of biomolecules, cells and microorganisms. In one aspect, the invention provides a compound having a maximal fluorescence excitation wavelength, wherein the compound has a structure of Formula II: ##STR00001##
wherein Z.sup.− is a counterion, Y is a bridge unit permitting electron delocalization between F and Ψ, and F is a moiety having the structure: ##STR00002## The present invention also provides various methods of using the fluorescent dyes for research and development, forensic identification, environmental studies, diagnosis, prognosis, and/or treatment of disease conditions.