Creating the PRLR recombinant monoclonal antibody is a complex process with several stages involved. Initially, the PRLR monoclonal antibody is harvested, and its gene sequence is determined. Subsequently, a vector carrying the PRLR monoclonal antibody gene is constructed and introduced into a host cell line for culture. During the PRLR monoclonal antibody production, a recombinant human PRLR protein is used as an immunogen. The PRLR recombinant monoclonal antibody is then purified using affinity chromatography and assessed for specificity using ELISA. It can react with human and mouse PRLR proteins.

The PRLR protein is a transmembrane protein expressed on the surface of many cell types in various tissues, including the breast, ovary, prostate, liver, and brain. When the hormone prolactin binds to the PRLR, it activates downstream signaling pathways that regulate cell proliferation, differentiation, and survival. The PRLR is also involved in the regulation of milk production in the mammary gland during lactation, as well as in the development and function of the reproductive system. Abnormal signaling through the PRLR has been implicated in various diseases, including breast and prostate cancer, infertility, and autoimmune disorders.

In yeast, fly, and mammalian cells, PCYT1A, the rate-limiting enzyme of phosphatidylcholine (PC) synthesis, is intranuclear and re-locates to the nuclear membrane in response to the demand for membrane PL production. Membrane lipid stored curvature elastic (SCE) stress is increased by PC deficiency. PCYT1A deletions caused functional impairment in cells that generate PC for secretion as well as membrane maintenance. Lipodystrophy, spondylometaphyseal dysplasia with cone-rod dystrophy (SMD-CRD), and isolated retinal dystrophy are all caused by mutations in the PCYT1A gene.

The development of the DLL3 recombinant monoclonal antibody involves a meticulous step-by-step process to ensure its exceptional quality and specificity. Initially, B cells are isolated from the spleen of an immunized animal, with the recombinant human DLL3 protein used as the immunogen. The RNA extracted from the B cells is converted into cDNA through reverse transcription. The DLL3 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, enabling the production of the DLL3 recombinant monoclonal antibody. After 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 various applications. Rigorous characterization assays, including ELISA and FC analysis, are performed to validate the antibody's specificity and functionality in detecting human DLL3 protein.

The creation of the MAPT recombinant monoclonal antibody is an intricate process that involves multiple steps. Initially, the MAPT monoclonal antibody is extracted and its gene sequence is determined. Following that, a vector carrying the MAPT monoclonal antibody gene is created and transfected into a host cell line for culture. To produce the MAPT monoclonal antibody, a recombinant human MAPT protein is utilized as an immunogen. The MAPT recombinant monoclonal antibody is subsequently purified through affinity chromatography, and its specificity is verified using ELISA. In the functional ELISA, this MAPT recombinant monoclonal antibody can bind to the mouse Mapt protein (CSB-MP013481MO) with the EC₅₀ of 436.1-518.6 ng/ml. It can react with mouse and macaca mulatta MAPT proteins.

The MAPT protein is mainly involved in the regulation and stabilization of microtubules in neurons. It is also important for maintaining the structure and function of neurons, particularly in the axons where it helps to establish and maintain the proper connections between neurons. Abnormalities in the MAPT protein have been linked to a number of neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. In these disorders, the MAPT protein can accumulate in the brain, forming structures called neurofibrillary tangles, which are a hallmark of these diseases.

The synthesis of the NECTIN4 recombinant monoclonal antibody involves a rigorous and precise process to ensure its exceptional quality and specificity. It begins with the isolation of B cells from an immunized animal, using the recombinant human NECTIN4 protein as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The NECTIN4 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 NECTIN4 recombinant monoclonal antibody. After 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 a wide range of applications. To ensure its reliability and functionality, the antibody undergoes ELISA to validate its specificity in detecting human NECTIN4 protein.

The synthesis of the ROR1 recombinant monoclonal antibody involves a meticulous process to ensure its exceptional quality and specificity. It begins with the isolation of B cells from an immunized animal, where the recombinant human ROR1 protein is used as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The ROR1 antibody genes are then amplified using specific primers designed for the antibody constant regions and inserted into an expression vector. Following transfection, the vector is introduced into host cells, enabling the production of the ROR1 recombinant monoclonal antibody. After cell culture, the antibody is harvested from the supernatant and purified using affinity chromatography, resulting in a highly purified form suitable for diverse applications. Rigorous characterization assays, including ELISA and FC analysis, are performed to validate the antibody's specificity and functionality in detecting human ROR1 protein.

CUSABIO conducted a meticulous production process to generate the MS4A1 recombinant monoclonal antibody. First, B cells were isolated from the spleen of an immunized animal, using recombinant human MS4A1 protein as the immunogen. Following that, RNA was extracted from the B cells and converted into cDNA through reverse transcription. Using the cDNA as a template, the gene encoding the MS4A1 antibody was amplified with a degenerate primer and inserted into a vector. The recombinant vector was then transfected into host cells to facilitate efficient antibody expression. The MS4A1 recombinant monoclonal antibodies were harvested from the cell culture supernatant and purified using affinity chromatography. This antibody shows reactivity with human and dog MS4A1 protein in ELISA.

CUSABIO employed a meticulous procedure to produce the DDR1 recombinant monoclonal antibody. Initially, B cells were isolated from the immunized animal's spleen, utilizing recombinant human DDR1 protein as the immunogen. Subsequently, RNA was extracted from the B cells and converted into cDNA through reverse transcription. Using the cDNA as a template, the gene encoding the DDR1 antibody was extended using a degenerate primer through PCR and inserted into a vector. The recombinant vector was then introduced into host cells through transfection, enabling efficient antibody expression. The DDR1 recombinant monoclonal antibodies were harvested from the cell culture supernatant and subjected to purification via affinity chromatography. Rigorous validation, including ELISA testing, was conducted to confirm this antibody's specific reactivity with human DDR1 protein, ensuring its reliability and suitability for a range of applications.

CUSABIO meticulously created the ZG16B recombinant monoclonal antibody through a carefully executed process. Initially, B cells were removed from the spleen of an immunized animal, with the recombinant human ZG16B protein serving as the immunogen. Following that, RNA extraction from the B cells and reverse transcription of RNA was performed to obtain cDNA. Using the cDNA as a template, the gene encoding the ZG16B antibody was amplified with a degenerate primer and inserted into a vector, which was then introduced into host cells via transfection to facilitate efficient antibody expression. The ZG16B recombinant monoclonal antibodies were harvested from the cell culture supernatant and purified using affinity chromatography. This antibody is recommended for the detection of human ZG16B protein in ELISA.

CUSABIO meticulously generated the CLDN4 recombinant monoclonal antibody through a systematic approach. Initially, B cells were isolated from the spleen of an immunized animal, using the recombinant human CLDN4 protein as the immunogen during the immunization process. Following that, RNA was extracted from the B cells and reverse-transcribed into cDNA. By utilizing the cDNA as a template, the gene encoding the CLDN4 antibody was extended using a degenerate primer and inserted into a vector. The recombinant vector was then transfected into host cells, enabling the expression of the CLDN4 recombinant monoclonal antibodies. Subsequently, these antibodies were harvested from the cell culture supernatant and purified using affinity chromatography. ELISA was performed to confirm this antibody's reactivity with human CLDN4 protein, ensuring its specificity, reliability, and suitability for various applications.