The NPC1L1 recombinant monoclonal antibody is a highly specific antibody that recognizes the human protein NPC1L1. This NPC1L1 antibody was made by transfecting human NPC1L1 monoclonal antibody gene-vector clones into a cell line for in vitro expression, then purifying the antibody using affinity chromatography from the tissue culture supernatant (TCS). The human NPC1L1 monoclonal antibody was produced by immunizing mice with a human NPC1L1 synthetic peptide. The isotype of this NPC1L1 antibody is the same as rabbit IgG. Recommended applications for this NPC1L1 antibody are ELISA and IHC.

NPC1L1 is a multi-transmembrane protein that is involved in both dietary and biliary cholesterol absorption. It also aids in the maintenance of intestinal cholesterol homeostasis. The cholesterol absorption inhibitor class of drugs, of which ezetimibe is the first extensively used one, has identified NPC1L1 as the molecular target.

The DNA sequence corresponding to the CCR8 monoclonal antibody produced from the animals through recombinant human CCR8 immunization was cloned into the expression vector, which was further transfected into a cell line for in vitro expression. The product is the recombinant CCR8 monoclonal antibody. It specifically targets the CCR8 from human. It belongs to the human IgG1. The affinity-chromatography purification method was used to purify this CCR8 antibody. The flow cytometry analysis has been tested for this CCR8 antibody.

Joseph R. Campbell et al. found that selective ablation of regulatory T cells with an anti-DHFR antibody can potentiate anti-tumor immune responses as a monotherapy or in combination with other immunotherapies. Daniel O. Villarreal et al. showed that anti-DHFR monoclonal antibody therapy, in synergy with the Listeria monocytogenes–based immunotherapy, remarkably retarded the growth of the established tumor and prolonged survival.

The creation of the Claudin-18.2 recombinant monoclonal antibody involves a meticulous process to ensure its high quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal, with the recombinant human Claudin-18.2 protein serving as the immunogen. The RNA extracted from the B cells is converted into cDNA through reverse transcription. The Claudin-18.2 antibody genes are then amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. This vector is subsequently transfected into host cells, facilitating the production of the Claudin-18.2 recombinant monoclonal antibody. After a period of cell culture, the antibody is collected from the cell culture supernatant and purified using affinity chromatography, yielding a highly purified form suitable for diverse applications. Stringent characterization assays, including ELISA and FC analysis, are performed to validate the antibody's specificity and functionality in detecting human Claudin-18.2 protein. The meticulous production process guarantees the development of a reliable and effective Claudin-18.2 recombinant monoclonal antibody, which plays a vital role in various Claudin-18.2-related research.

The creation of the GCGR recombinant monoclonal antibody involves a meticulous process to ensure its exceptional quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal using the recombinant human GCGR protein as the immunogen. RNA is extracted from the B cells and converted into complementary DNA (cDNA) through reverse transcription. The GCGR antibody genes are amplified using specific primers designed for the antibody constant regions and then inserted into an expression vector. This vector is subsequently introduced into host cells through transfection, enabling the production of the GCGR recombinant monoclonal antibody. Following a period of cell culture, the antibody is harvested from the cell culture supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for various applications. The antibody's specificity and functionality have been validated in ELIAS for detecting human GCGR protein.

The generation of the CD74 recombinant monoclonal antibody involves a meticulous process to ensure its exceptional quality and specificity. It begins by isolating B cells from an immunized animal, where the recombinant human CD74 protein is used as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The CD74 antibody genes are then amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. Through transfection, the vector is introduced into host cells, allowing for the production of the CD74 recombinant monoclonal antibody. Following cell culture, the antibody is harvested from the supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for various applications. ELISA is performed to validate the antibody's specificity and functionality in detecting human CD74 protein. This rigorous production process ensures the generation of a reliable and effective CD74 recombinant monoclonal antibody, vital for diverse CD74-related research.

The production of the CXCR4 recombinant monoclonal antibody involves a complex procedure that includes various stages. First, the CXCR4 monoclonal antibody is harvested, and its gene sequence is analyzed. Next, the CXCR4 monoclonal antibody gene is incorporated into a plasmid vector and then transfected into a host cell line for culture. The immunogen used for the CXCR4 monoclonal antibody production is a recombinant human CXCR4 protein. The CXCR4 recombinant monoclonal is purified using affinity chromatography from cell culture supernatant, and its specificity is evaluated by performing ELISA. It can react to human CXCR4 protein.

CXCR4 is a G protein-coupled receptor protein that binds to the chemokine CXCL12. It plays a crucial role in cell migration, proliferation, and survival, particularly in immune cells and cancer cells. CXCR4 is involved in various physiological processes, including hematopoiesis, angiogenesis, organogenesis, and immune surveillance. Dysregulation of CXCR4 signaling has been associated with various diseases, including cancer, HIV infection, and inflammatory disorders.

The process of creating the DSG3 recombinant monoclonal antibody is complex and comprises several steps. Firstly, the DSG3 monoclonal antibody is obtained, and its gene sequence is determined. Then, a vector containing the DSG3 monoclonal antibody gene is produced and introduced into a host cell line for culture. A recombinant human DSG3 protein is utilized as an immunogen during DSG3 monoclonal antibody synthesis. The DSG3 recombinant monoclonal antibody is then purified via affinity chromatography and subjected to ELISA to evaluate its specificity. It reacts with human and mouse DSG3 proteins.

DSG3 protein is a transmembrane glycoprotein that plays a critical role in the formation and maintenance of desmosomes. Desmosomes are intercellular junctions that provide strong adhesive interactions between adjacent epithelial cells, which is important for the integrity and strength of tissues. DSG3 is specifically expressed in stratified squamous epithelia and is found predominantly in the upper layers of the epidermis, oral mucosa, and hair follicles. Mutations in the DSG3 gene have been associated with various autoimmune diseases, including pemphigus vulgaris, in which the immune system mistakenly attacks and damages desmosomes, leading to blistering and erosions of the skin and mucous membranes.