Analysis of Antibody Induction by Macrophages Treated with Human Proteins in Mice.

Background: Macrophages are essential cellular components in various body tissues and tumor microenvironments. The high infiltration of macrophages into the tumor microenvironment determines the importance of treatment of personalized macrophages with recombinant cytotoxic T-lymphocyte-associated protein 4 (rCTLA-4), programmed death-ligand 1 (rPD-L1), and programmed cell death protein 1 (rPD-1) proteins to block immune checkpoints.

Methods: We investigated the development of humoral immunity against CTLA-4, PD-L1, and PD-1 receptors by introducing macrophages treated with the corresponding proteins into mice.

Generation of Peptides for Highly Efficient Proximity Utilizing Site-Specific Biotinylation in Cells.

Protein tags are peptide sequences genetically embedded into a recombinant protein for various purposes, such as affinity purification, Western blotting, and immunofluorescence. Another recent application of peptide tags is in vivo labeling and analysis of protein-protein interactions (PPI) by proteomics methods. One of the common workflows involves site-specific in vivo biotinylation of an AviTag-fused protein in the presence of the biotin ligase BirA.

Application of Skyline for Analysis of Protein-Protein Interactions In Vivo.

Quantitative and qualitative analyses of cell protein composition using liquid chromatography/tandem mass spectrometry are now standard techniques in biological and clinical research. However, the quantitative analysis of protein-protein interactions (PPIs) in cells is also important since these interactions are the bases of many processes, such as the cell cycle and signaling pathways. This paper describes the application of Skyline software for the identification and quantification of the biotinylated form of the biotin acceptor peptide (BAP) tag, which is a marker of in vivo PPIs.

In Vivo Quantitative Estimation of DNA-Dependent Interaction of Sox2 and Oct4 Using BirA-Catalyzed Site-Specific Biotinylation.

Protein-protein interactions of core pluripotency transcription factors play an important role during cell reprogramming. Cell identity is controlled by a trio of transcription factors: Sox2, Oct4, and Nanog. Thus, methods that help to quantify protein-protein interactions may be useful for understanding the mechanisms of pluripotency at the molecular level.

Triple Immunochromatographic System for Simultaneous Serodiagnosis of Bovine Brucellosis, Tuberculosis, and Leukemia.

An immunochromatographic test system has been developed for the simultaneous rapid multiplex serodiagnostics of bovine brucellosis, tuberculosis, and leukemia. The test system is based on the use of a conjugate of gold nanoparticles with the chimeric protein Cysteine-A/G and three analytical zones with immobilized pathogen antigens: lipolysaccharide, recombinant proteins MPB64 and MPB83-MPB63 of , and recombinant protein p24 of the bovine leukemia virus. Prototypes of the test system were tested on 98 samples of sera from healthy and infected animals.

[STUDY OF HEPATOPROTECTIVE PROPERTIES OF RNA-CONTAINING DRUG "RN-13" ON THE MODEL OF ACUTE TETRAHLLORMETHANE INDUCED HEPATITIS IN RATS].

The aim of the study was to assess the hepatoprotective properties of the RNA-containing drug RN-13 on the model of acute CLL4 induced hepatitis in rats. To evaluate hepatoprotective properties of the RNA-containing drug RN-13 42 female rats were used. RN-13 increases the survival rate of animals with acute tetrachloromethane hepatitis.