Compositions and methods related to Cas proteins, nucleic acids encoding the Cas proteins, and modified host cells comprising the Cas proteins and/or encoding nucleic acids are disclosed. Cas proteins are useful in a variety of applications. Cas proteins bind guide RNAs that in turn provide functional specificity to the Cas proteins, nucleic acids encoding the Cas guide RNAs, and modified host cells comprising the Cas guide RNAs and/or encoding nucleic acids. The Cas polypeptides and corresponding guide RNAs can be used in a variety of applications.

Site-specific modification of proteins with microbial transglutaminase (MTG) is a powerful and versatile strategy for a controlled modification of proteins under physiological conditions. We present evidence that solid-phase microbead-immobilization can be used to site-specifically and efficiently attach different functional molecules important for further downstream applications to proteins of therapeutic relevance including scFV, Fab-fragment and antibodies. We demonstrate that MTG remained firmly immobilized with no detectable column bleeding and that enzyme activity was sustained during continuous operation, which allowed for a convenient recycling of the enzyme, thus going beyond solution-phase MTG conjugation. In addition it is showed that immobilized MTG shows enhanced selectivity towards a certain residue in the presence of several reactive residues which are all targeted if the conjugation was carried out in solution. It is also reported on the site-specific lysine conjugation of antibodies using potent glutamine containing peptides with immobilized and MTG in solution. In addition, the generation of dual site-specifically conjugated IgG1 with immobilized and MTG in solution is reported, i.e. site-specific conjugation to glutamine and lysine residues of IgG1 antibody. Site-specific glutamine conjugation with small peptides containing a lysine residue and a functional moiety is also described.

Site-specific modification of proteins with microbial transglutaminase (MTG) is a powerful and versatile strategy for a controlled modification of proteins under physiological conditions. We present evidence that solid-phase microbead-immobilization can be used to site-specifically and efficiently attach different functional molecules important for further downstream applications to proteins of therapeutic relevance including scFV, Fab-fragment and antibodies. We demonstrate that MTG remained firmly immobilized with no detectable column bleeding and that enzyme activity was sustained during continuous operation, which allowed for a convenient recycling of the enzyme, thus going beyond solution-phase MTG conjugation. In addition it is showed that immobilized MTG shows enhanced selectivity towards a certain residue in the presence of several reactive residues which are all targeted if the conjugation was carried out in solution. It is also reported on the site-specific lysine conjugation of antibodies using potent glutamine containing peptides with immobilized and MTG in solution. In addition, the generation of dual site-specifically conjugated IgG1 with immobilized and MTG in solution is reported, i.e. site-specific conjugation to glutamine and lysine residues of IgG1 antibody. Site-specific glutamine conjugation with small peptides containing a lysine residue and a functional moiety is also described.

Described herein are methods of producing biosynthetic bacterial cellulose membranes having improved characteristics that are advantageous for use in various biological applications, including medicine.

The invention concerns a method for determining the reaction of at least one bacterium of interest to its exposure to an antibiotic implementing a Raman spectroscopy analysis comprising the following steps: Having a biological sample that could contain said bacteria of interest, Preparing at least two fractions of said sample each comprising one or more living bacteria of interest, Capturing, in each fraction, at least one living bacterium of interest by using a binding partner, Exposing at least one of the fractions to at least one concentration of at least one given antibiotic, the other of the fractions being the control fraction, Submitting the bacterium/bacteria of interest contained in the fractions to an incident light and analyzing the resultant light obtained by Raman diffusion by the bacterium/bacteria of interest by Raman spectroscopy in order to obtain as many Raman spectra as bacteria, Treating said spectra in order to obtain a signature of the reaction of the or each bacterium/bacteria of interest to the exposure to said antibiotic and of the control, Comparing the signature obtained accordingly per bacterium of interest to a reference base defined under the same conditions as above, for different bacteria and at least said antibiotic, and Defining a sensitivity clinical profile of said bacterium of interest to said antibiotic.

The present invention relates to a method for preparing poloxamer-protein particles. It also relates to poloxamer-protein particles obtainable by this method, dispersion thereof, and their use in methods of encapsulation, in particular of microencapsulation.

A cell printing apparatus according to the present disclosure comprises: a nozzle through which a liquid cell substance is discharged; a container in which the liquid cell substance discharged through the nozzle is laminated into a three-dimensional structure; and a supply unit for supplying the liquid heated to a predetermined temperature to the container.

Provided are: a cell tray provided with a concave part for supporting a cell aggregate and a hole formed on the bottom of the concave part; and a device for producing a cell structure, said device being provided with the cell tray and a puncture part passing through the cell tray and the cell aggregate, characterized in that the puncture part passes through the cell aggregate supported by the concave part until the tip thereof intrudes into the hole. Also provided is a system for producing a cell structure, said system comprising: a determination part that examines the characteristics of cell aggregates; a fractionation part that classifies the cell aggregates depending on the results of the examination by the determination part; a discharge part that disposes the cell aggregates in a cell tray depending on the results of the classification by the fractionation part; a puncture part that pass through a plurality of cell aggregates disposed in the cell tray; and a holding part that aligns and holds a plurality of puncture parts passing through a plurality of cell aggregates.

Provided are: a cell tray provided with a concave part for supporting a cell aggregate and a hole formed on the bottom of the concave part; and a device for producing a cell structure, said device being provided with the cell tray and a puncture part passing through the cell tray and the cell aggregate, characterized in that the puncture part passes through the cell aggregate supported by the concave part until the tip thereof intrudes into the hole. Also provided is a system for producing a cell structure, said system comprising: a determination part that examines the characteristics of cell aggregates; a fractionation part that classifies the cell aggregates depending on the results of the examination by the determination part; a discharge part that disposes the cell aggregates in a cell tray depending on the results of the classification by the fractionation part; a puncture part that pass through a plurality of cell aggregates disposed in the cell tray; and a holding part that aligns and holds a plurality of puncture parts passing through a plurality of cell aggregates.

Provided herein are perfusion fluids for enzymatically cleaving A-antigens from a donor organ, and methods. uses. associated therewith. In particular, the perfusion fluids comprise two enzymes. GalNAcDeacetylase and Galactosaminidase and the fluids may further comprise a buffered extracellular solution and/or a crowing agent. Furthermore. the compositions described herein were found to have activity at temperatures and ph levels suitable for cell viability.