The production of the IL17A monoclonal antibody started by using recombinant human IL17A protein as an immunogen. The cDNA of IL17A monoclonal antibody was sequenced and the gene was cloned into a plasmid vector. The plasmid vector containing the IL17A monoclonal antibody gene was then transfected into a host cell using a suitable transfection method. The resulting IL17A recombinant monoclonal antibody was purified using affinity chromatography and its specificity was tested using ELISA. It only reacts with human IL17A protein. It was found to bind specifically to the recombinant human IL17A(CSB-BP624104HU(M)) with an EC₅₀ range of 1.818-2.170 ng/mL.

IL17A is a cytokine protein produced by various immune cells, including T helper 17 (Th17) cells and other cell types such as γδ T cells, natural killer (NK) T cells, and some innate lymphoid cells. The main function of IL-17A is to induce inflammatory responses, particularly in the context of defense against bacterial and fungal infections. It promotes the recruitment and activation of neutrophils and other immune cells to sites of infection, as well as the production of pro-inflammatory cytokines and chemokines. IL-17A has also been implicated in the pathogenesis of several autoimmune and inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and psoriasis.

The TROP2 monoclonal antibody was produced by immunizing with recombinant human TROP2 protein. The gene encoding the TROP2 monoclonal antibody was cloned into a plasmid vector after sequencing the cDNA. Transfection of the host cell with the plasmid vector containing the TROP2 monoclonal antibody gene was performed using a suitable transfection method. The affinity chromatography purification of the resulting TROP2 recombinant monoclonal antibody was carried out, and its specificity was tested in ELISA. This TROP2 recombinant monoclonal antibody showed the ability to bind specifically to recombinant human TROP2 (CSB-MP023072HU1d7) with an EC₅₀ range of 0.7284-1.075 ng/mL. It can react with human TROP2 protein.

TROP2, also known as TACSTD2, is a transmembrane glycoprotein expressed in various human tissues and plays a role in cell adhesion, migration, and proliferation. It is involved in the regulation of cell growth and differentiation and has been shown to be upregulated in many types of cancer, including breast, colorectal, lung, and ovarian cancer. TROP2 overexpression is associated with tumor growth, metastasis, and poor patient prognosis. Additionally, TROP2 has been identified as a target for cancer immunotherapy.

The creation of the LY6G6D recombinant monoclonal antibody involves the following steps: 1. LY6G6D antibody generation. Use the recombinant human LY6G6D protein as the immunogen to induce an immune reaction and harvest B cells. 2. Gene cloning. Extract total RNA from the harvested B cells. Convert the RNA into cDNA using reverse transcription. Amplify the LY6G6D antibody genes using PCR with primers specific to the antibody constant regions. Clone the antibody genes into an expression vector. 3. Recombinant antibody expression and purification. Transfect the expression vector containing the LY6G6D antibody genes into host cells for antibody expression. Collect the cell culture supernatant and purify the LY6G6D recombinant monoclonal antibody using affinity chromatography. 4. Antibody characterization and validation. This purified antibody has been tested to recognize and bind to the human and macaca fascicularis LY6G6D protein in ELISA and FC.

The GLP1R recombinant monoclonal antibody was produced by CUSABIO using the following steps: First, B cells were separated from the spleen of the immunized animal. The immunization process involved using recombinant human GLP1R protein as the immunogen. Next, RNA was isolated from the B cells, followed by reverse transcription to synthesize cDNA. Using the cDNA as a template, the gene encoding the GLP1R antibody was extended using a degenerate primer. The GLP1R antibody was inserted into a vector. The recombinant vector was introduced into host cells through transfection, allowing the host cells to express the GLP1R recombinant monoclonal antibody. The GLP1R recombinant monoclonal antibodies were harvested from the cell culture supernatant and subsequently purified using affinity chromatography. Finally, these purified antibodies have been demonstrated to recognize the human GLP1R protein in ELISA.

The IL8 recombinant monoclonal antibody is generated through in vitro processes using synthetic genes. After the extraction of the IL8 antibody genes from B cells that are isolated from immunoreactive rabbits, these genes are amplified and cloned into appropriate phage vectors. These vectors are then introduced into mammalian cell lines, enabling the production of functional antibodies. Subsequently, the IL8 recombinant monoclonal antibody is purified through affinity chromatography. After rigorous verification, the antibody can be used in ELISA and FC applications to detect the human IL8 protein.

IL-8 is a pro-inflammatory chemokine that plays a central role in the immune response and inflammatory processes. Its functions include the recruitment and activation of immune cells, inflammation induction, angiogenesis, and immune cell trafficking. While IL-8 is crucial for the body's defense against infections and tissue repair, dysregulation of its activity can contribute to inflammatory diseases and cancer.

The SAA1 recombinant monoclonal antibody is synthetically generated in vitro, starting with the extraction of SAA1 antibody genes from B cells isolated from immunoreactive rabbits. These genes are then amplified and cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to enable the production of functional antibodies. After that, the SAA1 recombinant monoclonal antibody undergoes affinity chromatography purification. This antibody is suitable for the detection of human SAA1 protein in ELISA and FC applications.

SAA1 is an acute-phase protein that plays a crucial role in the body's response to inflammation and infection. It functions as an inflammation marker, lipid transporter, immune modulator, and potentially, a contributor to tissue repair and pathogenic amyloid formation. Its dysregulation is associated with various inflammatory conditions and diseases.

The APOL1 recombinant monoclonal antibody is generated through in vitro processes using synthetic genes. This methodology involves the retrieval of APOL1 antibody genes from B cells sourced from immunoreactive rabbits, followed by their amplification and cloning into appropriate phage vectors. These vectors are then introduced into mammalian cell lines, enabling the production of functional antibodies in substantial quantities. Subsequently, the APOL1 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It is recommended for the detection of human APOL1 protein in ELISA and FC applications.

APOL1 is a member of the apolipoprotein family and is primarily found in the bloodstream. The main role of APOL1 is to provide protection against African trypanosomes by participating in the innate immune response. Its lytic activity, when functioning effectively, helps to control trypanosome infections.

The USP22 recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, USP22 antibody genes are extracted from B cells isolated from immunoreactive rabbits. These genes undergo amplification and are cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies in significant quantities. The resulting USP22 recombinant monoclonal antibody is subjected to affinity chromatography purification. After rigorous verification, the antibody can be used in ELISA, IF, and FC applications, allowing for precise detection of human USP22 protein.

USP22 is a multifunctional protein that plays a crucial role in epigenetic regulation by deubiquitinating histones and modulating chromatin structure. Its activities impact gene expression, cell cycle control, stem cell maintenance, DNA repair, and various aspects of development. Dysregulation of USP22 can have significant implications for diseases, including cancer.

The INHBB recombinant monoclonal antibody is synthesized in vitro through a systematic process. Initially, INHBB antibody genes are isolated from B cells derived from immunoreactive rabbits. These genes undergo amplification and are cloned into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the generation of functional antibodies in significant quantities. The resulting INHBB recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. This antibody shows reactivity with human INHBB protein and has been validated in ELISA and FC applications.

INHBB is a critical component in the formation of inhibin and activin, two hormone complexes that play essential roles in regulating the endocrine and reproductive systems, as well as aspects of embryonic development and tissue homeostasis. These functions are vital for maintaining hormonal balance and proper functioning of the reproductive system.

The CASP3 recombinant monoclonal antibody is synthetically generated in vitro, starting with the extraction of CASP3 antibody genes from B cells isolated from immunoreactive rabbits. These genes are then amplified and cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to enable the production of functional antibodies in substantial quantities. Following this, the CASP3 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. This antibody can react with human CASP3 protein and has been tested for ELISA, WB, and IHC applications.

CASP3 is a critical enzyme in apoptosis, serving as an executioner that dismantles and disposes of cells in a controlled and regulated manner. Its role is essential for tissue development, maintenance of tissue homeostasis, and preventing the survival of damaged or harmful cells.