Abstract: This invention provides ink particles comprising a) a core comprising a coloring agent and a polymer, and b) an outermost layer comprising a surfactant or a dispersant, wherein the core further comprises an outer surface and the outermost layer at least partially covers the outer surface of the core.

Abstract: The disclosure relates to a composition that is designed to be administered to a subject intradermally for treating pigmentless skin or creating a temporary tattoo. The composition comprises particles having a polymeric shell and a core that includes a coloring agent. The particles are in a carrier solution at a concentration that is cosmetically effective to delay the bioabsorbance and/or biodegradation of coloring agent in a subject's skin. Bioabsorbance and/or biodegradation of the particles fades the tattoo until it is no longer visible.

Abstract: A method for designing circular permuted proteins using two engineered Mu transposons for easy construction of random circular permuted proteins, the two designed transposons being MuCP-ISC (Mu Circular permutation transposon with Integrated Start Codon) and MuCP-ISSC (Mu Circular permutation transposon with Integrated Start and Stop Codon).

Abstract: A method for designing circular permuted proteins using two engineered Mu transposons for easy construction of random circular permuted proteins, the two designed transposons being MuCP-ISC (Mu Circular permutation transposon with Integrated Start Codon) and MuCP-ISSC (Mu Circular permutation transposon with Integrated Start and Stop Codon).

Abstract: Methods for facile construction of a random domain insertion library (1) with optimal control of composition and length of inter-domain linker residues and (2) mediated by sticky-end ligation between host and guest DNA fragments. To develop such a method, we engineered a Mu transposon. The method exploits transposition of the engineered Mu transposon, which, upon removal, allows for sticky-end ligation between host and guest DNA fragments. We used a gene coding for xylanase from bacillus circulans (BCX) as a guest DNA sequence and the plasmid PUC19 containing lacZ? as the target for insertion (i.e., a host DNA sequence). Results demonstrate that the method enables facile construction of a random domain insertion library with optimal control of composition and length of inter-domain linker residues.

Abstract: Methods for facile construction of a random domain insertion library (1) with optimal control of composition and length of inter-domain linker residues and (2) mediated by sticky-end ligation between host and guest DNA fragments. To develop such a method, we engineered a Mu transposon. The method exploits transposition of the engineered Mu transposon, which, upon removal, allows for sticky-end ligation between host and guest DNA fragments. We used a gene coding for xylanase from bacillus circulans (BCX) as a guest DNA sequence and the plasmid PUC19 containing lacZ? as the target for insertion (i.e., a host DNA sequence). Results demonstrate that the method enables facile construction of a random domain insertion library with optimal control of composition and length of inter-domain linker residues.

Abstract: A strategy to improve protein stability by domain insertion. TEM 1 beta-lactamase (BLA) and exo-inulinase, as model target enzymes, are inserted into a hyperthermophilic maltose binding protein from Pyrococcus furiosus (PfMBP). Unlike conventional protein stabilization methods that employ mutations and recombinations, the inventive approach does not require any modification on a target protein except for its connection with a hyperthermophilic protein scaffold. For that reason, target protein substrate specificity was largely maintained, which is often modified through conventional protein stabilization methods. The insertion was achieved through gene fusion by recombinant DNA techniques.

Abstract: A strategy to improve protein stability by domain insertion. TEM 1 beta-lactamase (BLA) and exo-inulinase, as model target enzymes, are inserted into a hyperthermophilic maltose binding protein from Pyrococcus furiosus (PfMBP). Unlike conventional protein stabilization methods that employ mutations and recombinations, the inventive approach does not require any modification on a target protein except for its connection with a hyperthermophilic protein scaffold. For that reason, target protein substrate specificity was largely maintained, which is often modified through conventional protein stabilization methods.