The generation of the SEMA4D recombinant monoclonal antibody involves a series of steps. Initially, the SEMA4D monoclonal antibody is harvested and its gene sequence is determined. A vector containing the SEMA4D monoclonal antibody gene is subsequently constructed and transfected into a host cell line for culturing. The synthesis of the SEMA4D monoclonal antibody employs a recombinant human SEMA4D protein as an immunogen. Finally, the SEMA4D recombinant monoclonal antibody is purified through affinity chromatography and analyzed for specificity using ELISA and FC assays. It only reacts with human SEMA4D protein.

SEMA4D is a protein that belongs to the semaphorin family, which plays a crucial role in cell signaling and regulation of various physiological processes, including cell migration, axon guidance, and immune responses. SEMA4D acts as both a ligand and a receptor, interacting with a variety of other proteins, including plexin B1, CD72, CD100, and integrins. These interactions activate intracellular signaling pathways, leading to changes in cell behavior, such as cell adhesion, cell migration, proliferation, and survival. In the immune system, SEMA4D plays a role in regulating immune cell function. It can also modulate immune cell activity by regulating cytokine production, phagocytosis, and antigen presentation. SEMA4D has been implicated in various physiological and pathological processes, including cancer, inflammation, cardiovascular diseases, and neurological disorders.

The generation of the TNFRSF9/4-1BB recombinant monoclonal antibody involves a meticulous and controlled process to ensure its exceptional quality and specificity. It begins by isolating B cells from the spleen of an immunized animal, where the recombinant human TNFRSF9 protein is used as the immunogen. The extracted RNA from the B cells is converted into cDNA through reverse transcription. The TNFRSF9 antibody genes are then amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. This vector is subsequently transfected into host cells, allowing for the production of the TNFRSF9/4-1BB recombinant monoclonal antibody. After a period of cell culture, the antibody is harvested from the supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for various applications. ELISA is conducted to validate the antibody's specificity and functionality in detecting human TNFRSF9 protein. This stringent production process ensures the generation of a reliable and effective TNFRSF9 recombinant monoclonal antibody, essential for diverse TNFRSF9-related research and diagnostic applications.

The generation of the ANGPT2 recombinant monoclonal antibody involves a precise and thorough process to ensure its exceptional quality and specificity. It begins by isolating B cells from the spleen of an immunized animal, where the recombinant human ANGPT2 protein serves as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The ANGPT2 antibody genes are amplified using specific primers designed for the antibody constant regions and then inserted into an expression vector. Through transfection, the vector is introduced into host cells, enabling the production of the ANGPT2 recombinant monoclonal antibody. Following a period of cell culture, the antibody is harvested from the cell culture supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for a variety of applications. The antibody's specificity and functionality have been tested in ELISA for detecting human ANGPT2 protein. This meticulous production process ensures the production of a reliable and effective ANGPT2 recombinant monoclonal antibody, crucial for diverse ANGPT2-related research.

The process of generating the CD96 recombinant monoclonal antibody is complex and consists of several stages. Firstly, the CD96 monoclonal antibody is collected, and its gene sequence is analyzed. Next, a vector containing the CD96 monoclonal antibody gene is constructed and transfected into a host cell line for culturing. During the CD96 monoclonal antibody production, a recombinant human CD96 protein is used as an immunogen. The CD96 recombinant monoclonal antibody is then purified using affinity chromatography and assessed for specificity using ELISA applications. It can bind to the human CD96 protein (CSB-MP004971HU1(F2)) with the EC₅₀ of 95.78-127.1 ng/mL. It only recognizes the human species.

CD96, also known as TACTILE, is a transmembrane protein expressed on the surface of a variety of immune cells, including natural killer (NK) cells, T cells, and dendritic cells. CD96 is involved in the regulation of immune cell activation and plays a role in the recognition and elimination of target cells, including tumor cells. CD96 can bind to its ligand CD155, which is expressed on the surface of tumor cells and other target cells. This interaction leads to the activation of immune cells and the initiation of an immune response against the target cells. CD96 has also been implicated in the regulation of immune cell migration and the development of immune cell memory.

The creation of the CSF2RB recombinant monoclonal antibody involves a meticulous and controlled process to ensure its exceptional quality and specificity. It begins by isolating B cells from an immunized animal using the recombinant human CSF2RB protein as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The CSF2RB 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, enabling the production of the CSF2RB recombinant monoclonal antibody. After a period of cell culture, the antibody is collected from the supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for various applications. To ensure its reliability and functionality, CUSABIO conducts ELISA to validate its specificity and effectiveness in detecting human CSF2RB protein.

The creation of the GPRC5D recombinant monoclonal antibody follows a meticulous and precise process to ensure its exceptional quality and specificity. It begins with the isolation of B cells from an immunized animal, where the recombinant human GPRC5D protein is used as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The GPRC5D antibody genes are then amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. Through transfection, the vector is introduced into host cells, enabling the production of the GPRC5D recombinant monoclonal antibody. Following a period of cell culture, the antibody is harvested from the supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for diverse applications. CUSABIO performs ELISA to validate the antibody's specificity and functionality in detecting human GPRC5D protein.

The generation of the TFPI recombinant monoclonal antibody follows a meticulous process to guarantee its exceptional quality and specificity. It begins by isolating B cells from an immunized animal, with the recombinant human TFPI protein used as the immunogen. Total RNA is then extracted from these B cells and converted into cDNA through reverse transcription. The TFPI antibody genes are amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. This vector is transfected into host cells, enabling the production of the TFPI recombinant monoclonal antibody. After cell culture, the antibody is harvested from the supernatant and purified using affinity chromatography, resulting in a highly purified form ready for various applications. To ensure its reliability, ELISA is performed to validate the antibody's specificity and functionality in recognizing human and rabbit TFPI protein. This rigorous production process ensures the generation of a robust and effective TFPI recombinant monoclonal antibody, indispensable for a wide range of TFPI-related research.

CUSABIO employed a rigorous process to produce the CNR1 recombinant monoclonal antibody with utmost precision. Initially, B cells were isolated from the spleen of an immunized animal, utilizing the recombinant human CNR1 protein as the immunogen. Subsequently, RNA was extracted from the B cells and converted into cDNA through reverse transcription. With the cDNA as a template, the gene encoding the CNR1 antibody was amplified using a degenerate primer and inserted into a vector. The recombinant vector was then introduced into host cells via transfection, enabling the efficient expression of the CNR1 recombinant monoclonal antibodies. Following expression, these antibodies were harvested from the cell culture supernatant and subjected to a purification process using affinity chromatography. This antibody can recognize human CNR1 protein in ELISA.

The ENPP3 monoclonal antibody was generated using the recombinant human SLC39A6 protein as an immunogen. The cDNA of the ENPP3 monoclonal antibody was sequenced to obtain the antibody gene, which was cloned into a plasmid vector. The plasmid vector was then transfected into host cells using a suitable transfection method. The resulting ENPP3 recombinant monoclonal antibody underwent purification through affinity chromatography and was subsequently tested for specificity through ELISA. The antibody demonstrated binding capabilities to the recombinant human ENPP3 (CSB-MP4278MOV) with an EC₅₀ range of 3.313-4.724 ng/mL. It can react with human and macaca fascicularis ENPP3 proteins.

ENPP3 is a transmembrane glycoprotein that plays a role in the regulation of cell growth, differentiation, and mineralization. It is involved in the hydrolysis of extracellular nucleotides to generate inorganic phosphate and nucleoside diphosphates, which are important for the regulation of purinergic signaling pathways. ENPP3 is expressed in various tissues, including bone, kidney, and liver, and its dysregulation has been linked to a number of diseases, including calcification disorders, cancer, and inflammation.

The GPC3 recombinant monoclonal antibody was meticulously produced by CUSABIO using a systematic approach. Initially, isolating B cells from the spleen of an immunized animal. The recombinant human GPC3 protein was used as the immunogen. Following this, extracting RNA from the B cells and converting it into cDNA through reverse transcription. Using the cDNA as a template, the gene encoding the GPC3 antibody was amplified with a degenerate primer and inserted into a vector. This recombinant vector was then transfected into host cells, facilitating the expression of the GPC3 recombinant monoclonal antibodies. These antibodies were subsequently harvested from the cell culture supernatant and purified using affinity chromatography. It has been confirmed that this antibody can detect human GPC3 protein in ELISA.