The present invention relates to engineered a cytolytic immune cell comprising: i) a releasable protein which comprises a polypeptide of interest (POI) and a first interaction domain; and ii) a retention protein which is retained within an intracellular compartment of the cell and comprises a second interaction domain which binds to the first protein interaction domain, wherein binding between the first protein interaction domain and second protein interaction domain is disrupted by the presence of an agent, such that in the absence of the agent, the first protein interaction domain and second protein interaction domain bind and result in retention of the POI within an intracellular compartment; whereas in the presence of the agent, the first protein interaction domain and second protein interaction do not bind and the POI is released from the intracellular compartment and expressed at the cell surface or secreted by the cell.

The present invention provides engineered immune cells comprising an anti-CD2 protein expression blocker (PEBL) and an anti-CD2 chimeric antigen receptor (CAR). In some embodiments, such engineered immune cells lack surface expression CD2. Also, provided herein are methods of using such cells in cancer therapies.

Provided herein are NK-92 cells expressing at least one CAR and at least one Fc receptor. Also provided are methods of treatment of a patient having or suspected of having a disease that is treatable with NK-92 cells, such as cancer, comprising administering to the patient NK-92-Fc-CAR.

The present invention refers to a fluorescent fusion polypeptide capable of changing its localization within the cell from the cell cytoplasmic membrane to the retention vesicles, upon an increase in the concentration of second messengers within the cell cytoplasm, comprising a membrane localization peptide, a second messenger transduction protein binding peptide, a reticulum retention signal and a fluorescent peptide wherein: a. the membrane localization peptide is located at the N-terminus of the fluorescent fusion polypeptide and is physically bound, optionally through a linker, to the fluorescent peptide, which in turn is physically bound, optionally through a linker, to the second messenger transduction protein binding peptide; and b. the second messenger transduction protein binding peptide is physically bound, optionally through a linker, to the reticulum retention signal, which in turn is located at the C-terminus of the fluorescent fusion polypeptide.

The present invention refers to a fluorescent fusion polypeptide capable of changing its localization within the cell from the cell cytoplasmic membrane to the retention vesicles, upon an increase in the concentration of second messengers within the cell cytoplasm, comprising a membrane localization peptide, a second messenger transduction protein binding peptide, a reticulum retention signal and a fluorescent peptide wherein: a. the membrane localization peptide is located at the N-terminus of the fluorescent fusion polypeptide and is physically bound, optionally through a linker, to the fluorescent peptide, which in turn is physically bound, optionally through a linker, to the second messenger transduction protein binding peptide; and b. the second messenger transduction protein binding peptide is physically bound, optionally through a linker, to the reticulum retention signal, which in turn is located at the C-terminus of the fluorescent fusion polypeptide.

Provided is a technique for highly expressing a target protein in a plant cell by using a glycosylation domain, a recombinant vector comprising a gene encoding a fusion protein of a glycosylation domain and a target protein, a recombinant cell, a transformed plant, and a method of producing a target protein using these.

The present disclosure relates to the design of a recombinant vector for production and separation/purification of a carbonic anhydrase in a plant, a method of separating and purifying a recombinant protein including a carbonic anhydrase produced in a plant by using the capacity of a CBM3 domain of the recombinant protein to bind to cellulose beads, and a method of inducing the hydration reaction of carbon dioxide using a carbonic anhydrase in a state of being firmly immobilized onto the surfaces of cellulose beads by CBM3.

The present invention relates to a fusion protein consisting of a scFv linked to a horseradish peroxidase enzyme or to an alkaline phosphatase enzyme by a peptide linker. The fusion protein also includes a histidine tag and optionally an endoplasmic reticulum retention signal. The invention also includes nucleic acids encoding the fusion protein, expression vectors containing the nucleic acids, plant cells transformed with the expression vectors and methods of producing the fusion proteins of the invention.

The invention relates to protein-based T-cell receptor knockdown, and its use in T-cell therapies.

The present invention relates to a hook fusion protein comprising a hook domain and at least one cytoplasmic carboxy terminal endoplasmic reticulum (ER) retention signal and/or at least one cytoplasmic amino terminal endoplasmic reticulum (ER) retention signal; wherein the hook fusion protein is a soluble protein that localizes in the cytoplasm. The present invention also relates to a nucleic acid system for intracellular targeting control comprising a nucleic acid encoding a hook fusion protein as herein disclosed, and a nucleic acid encoding a target fusion protein comprising a hook-binding domain; wherein said target fusion protein in a membrane protein; and wherein the hook fusion protein localizes in the ER when bound to the target fusion protein. The invention also encompasses a vector system, viral particle system, host cell and kit comprising said nucleic acids. The invention also includes the vector system, viral particle system, host cell or kit for use as a medicament, in particular for immunotherapy.