Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, most of the mice show no toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, no mice shows toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-tetrodotoxin humanized antibody Y126C and use thereof. The humanized antibody has a heavy-chain variable region and a light-chain variable region with amino acid sequences shown in SEQ ID NO: 1 to SEQ ID NO: 2, respectively. Affinity analysis shows that the antibody of the present disclosure has prominent affinity. It is proved by experiments that, after mice in an antibody protection group pre-injected with the antibody of the present disclosure are injected with tetrodotoxin, most of mice do not show toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the antibody of the present disclosure shows excellent anti-tetrodotoxin effects, excellent preventive or therapeutic effects on puffer fish-related biological injuries, and promising clinical application prospects.

Abstract: A chimeric antigen receptor (CAR) cell library is established through the fusion of a cell and a vector assembly. The vector assembly carries three genetic elements corresponding to a plurality of first genetic elements encoding one or more idiotype CARs, a second genetic element carrying one or more genetic circuits, and a third genetic element encoding one or more inducible proteins, respectively. The one or more genetic circuits are pre-programmed and are each a combination of a cis-regulatory factor and a transcription factor; and the one or more inducible proteins include one or two selected from the group consisting of a drug resistance protein and a suicide protein. By designing a CAR library-genetic circuit-inducible protein coupling scheme, the cell library construction and screening for complex and unknown disease target antigens are realized, such as to solve the problems that there are complex, diverse, and variable antigens.

Abstract: The present disclosure relates to the technical field of biomedicine, and provides an anti-physaliatoxin nanobody, and a preparation method and use thereof. The nanobody is a VHH antibody with an amino acid sequence shown in SEQ ID NO. 1. Affinity analysis shows that the nanobody of the present disclosure has prominent affinity. It is proved by small animal experiments that, after mice in an antibody protection group pre-injected with the nanobody of the present disclosure are injected with physaliatoxin, no mice shows toxic symptoms, and during continuous observation for one month, no toxic lethality occurs, indicating that the nanobody of the present disclosure shows excellent anti-physaliatoxin effects, excellent preventive or therapeutic effects on jellyfish stings, and promising clinical application prospects.

Abstract: An application of a RyR2 protein or a recombinant RyR2 protein in preparing an anti-heart failure medicament is provided. The recombinant RyR2 protein is a naturally occurring RyR2 protein fragment or a mutant, such as a SPRY1 domain protein, a P1 domain protein, a SPRY2 domain protein, a SPRY3 domain protein, a Handle domain protein, an HD1 domain protein, an HD2 domain protein, a central domain protein, an EF-hand domain protein, a U-motif protein, a P2 domain protein, a P2 domain fragment protein-1, a P2 domain fragment protein-2 derived from a natural RyR2 protein or a P2 mutant derived from the natural RyR2 protein. The exogenous recombinant RyR2 protein is highly expressed in both normal small animal and diseased small animal models, so that the left ventricular ejection fraction of experimental animals is improved varying degrees compared with that of a control group.

Abstract: Provided are a method for preparing chimeric antigen receptor (CAR)-carrying exosomes derived from immune cells through isolation, and use of the CAR-carrying exosomes. The method includes: A) preparation of CAR expressing immune cells; B) antigen-specific activation of the CAR expressing immune cells; C) isolation of exosomes secreted by CAR expressing immune cells; and D) purification and enrichment of CAR exosomes. The immune cells in step A are T cells or NK cells; and the immune cells are derived from a patient or a healthy donor. CAR expressing immune cells are activated with specific antigens, and the resulting exosomes are further analyzed, isolated, purified and enriched to finally obtain CAR-carrying exosomes derived from immune cells. The exosomes can be used for treating cancer, severe infectious diseases, and other diseases.