The SLC39A6 monoclonal antibody was generated using recombinant human SLC39A6 protein as the immunogen. The SLC39A6 monoclonal antibody's DNA sequence was obtained through cDNA sequencing and cloned into a plasmid vector, which was then transfected into a host cell for expression. The resulting SLC39A6 recombinant monoclonal antibody was purified using affinity chromatography and its specificity was confirmed through ELISA. It only shows reactivity with human SLC39A6 protein. It demonstrated high affinity binding to the recombinant human SLC39A6 protein (CSB-BP621669HU) with an EC₅₀ range of 0.6873-0.9010 ng/mL.

The SLC39A6 protein, also known as ZIP6, plays a crucial role in the cellular uptake and distribution of zinc, which is essential for various cellular processes such as DNA synthesis, immune function, and cell division. SLC39A6 is expressed in a variety of tissues, including the liver, kidney, and brain, and has been implicated in the development and progression of several diseases, including cancer and neurodegenerative disorders.

The expression of WFDC2 recombinant monoclonal antibody typically involves the initial step of incorporating the WFDC2 antibody-encoding gene into expression vectors. These vectors are then introduced into host cells via polyethyleneimine-mediated transfection. Culturing of the host cells leads to the production and secretion of these antibodies. Post-affinity chromatography purification, the antibodies' functionality is evaluated using ELISA, WB, and FC assays, demonstrating their specific reactivity with the human WFDC2 protein.

WFDC2 is a protein with a primary role in ovarian function and reproductive biology. Its clinical significance lies in its use as a biomarker for ovarian cancer, aiding in early detection and monitoring, but it also has potential implications in other gynecological conditions and pregnancy.

The process for generating the CD247 recombinant monoclonal antibody typically begins with the incorporation of the CD247 antibody-encoding gene into expression vectors. These vectors are then transferred into host cells via polyethyleneimine. The host cells containing these vectors are cultured to produce and excrete the antibodies. After purification through affinity chromatography, the antibodies undergo evaluations involving ELISA and FC assays, demonstrating their specific binding to the human CD247 protein.

CD247 is a critical component of the TCR complex and plays a central role in T-cell activation and immune responses. It is essential for transmitting signals from the TCR to the interior of T cells, leading to their activation and proliferation in response to specific antigens.

The phospho-MAPT (S199) recombinant monoclonal antibody expression typically involves the initial step of inserting the MAPT antibody-encoding gene into expression vectors. These vectors are then introduced into host cells using polyethyleneimine-mediated transfection. Culturing of the host cells leads to the production and secretion of the antibodies. Post-affinity chromatography purification, the antibodies' functionality is assessed through ELISA, IHC, and FC tests, confirming their capacity to recognize the human MAPT protein phosphorylated at S199.

MAPT phosphorylated at S199 is intimately involved in microtubule regulation, neuronal morphology, and its association with neurodegenerative diseases, particularly Alzheimer's disease and tauopathies.

The production of the phospho-MAPT (S404) recombinant monoclonal antibody generally begins with the incorporation of the MAPT antibody-encoding gene into expression vectors. These vectors are then delivered into host cells through polyethyleneimine-mediated transfection. The host cells, housing the expression vectors, are cultured to generate and release the antibodies. Subsequent purification using affinity chromatography is followed by assessments through ELISA and IHC assays, verifying their ability to specifically bind to the human MAPT protein phosphorylated at S404.

MAPT phosphorylated at S404 represents a specific post-translational modification of the MAPT protein. Phosphorylation of MAPT at S404 is involved in the regulation of microtubules and neuronal function and is associated with neurodegenerative diseases, particularly Alzheimer's disease.

The phospho-MAPT (S214) recombinant monoclonal antibody generation typically starts with the insertion of the MAPT antibody-encoding gene into expression vectors. These vectors are subsequently introduced into host cells via polyethyleneimine-mediated transfection. The host cells, containing these vectors, are cultured to produce and release the antibodies. Following purification using affinity chromatography, the antibodies undergo testing through ELISA and IHC assays to confirm their recognition of the human MAPT protein phosphorylated at S214.

MAPT is a microtubule-associated protein that plays a crucial role in binding to and stabilizing microtubules, which are essential components of the neuronal cytoskeleton. Phosphorylation of MAPT at S214 can modulate the affinity of MAPT for microtubules and influence microtubule dynamics.

The expression of phospho-MAPT (S202) recombinant monoclonal antibody typically involves the initial step of incorporating the MAPT antibody-encoding gene into expression vectors. These vectors are then introduced into host cells via polyethyleneimine-mediated transfection. Subsequent culturing of the host cells leads to the production and secretion of these antibodies. After purification through affinity chromatography, the antibodies' functionality is evaluated using ELISA and FC assays, demonstrating their specific binding to the human MAPT protein phosphorylated at S202.

MAPT, when phosphorylated at S202 and other sites, can modulate the stability and dynamics of microtubules in neurons. Phosphorylation of MAPT at S202, in particular, is associated with tau hyperphosphorylation and aggregation, contributing to neuronal damage and cognitive decline in Alzheimer's disease.

Typically, PLAT recombinant monoclonal antibody production begins with the insertion of the PLAT antibody-encoding gene into expression vectors. Subsequently, these vectors are introduced into host cells using polyethyleneimine-mediated transfection. The cells housing the expression vectors are then cultured to generate and release the antibodies. After purification via affinity chromatography, the antibody's functionality is evaluated through ELISA and FC assays, demonstrating their ability to specifically bind to the human PLAT protein.

PLAT is a critical enzyme involved in the activation of plasminogen, leading to the breakdown of fibrin clots in the fibrinolytic pathway. This process is essential for maintaining vascular health, preventing thrombosis, and facilitating tissue repair and remodeling. The precise regulation of PLAT activity is crucial for maintaining a balance between clot formation and dissolution in the circulatory system.

The process for generating the MYO7A recombinant monoclonal antibody typically commences by inserting the MYO7A antibody-encoding gene into expression vectors. These vectors are subsequently delivered into host cells using the polyethyleneimine-mediated transfection method. The host cells containing these vectors are cultured to produce and excrete the antibodies. Post-affinity chromatography purification, the antibodies are subjected to assessments involving ELISA and FC tests, confirming their capacity to recognize the human MYO7A protein.

MYO7A is a multifunctional protein with diverse roles in cellular processes. Its primary functions include involvement in auditory and visual sensory functions, intracellular transport, maintenance of microvilli, cellular adhesion, vesicle trafficking, and melanosome transport. Mutations in the MYO7A gene can lead to various disorders affecting hearing, vision, and other cellular processes.

The recombinant human VSIG4 protein was used as the immunogen to produce the VSIG4 monoclonal antibody. Obtaining the DNA sequence of the VSIG4 monoclonal antibody by sequencing the cDNA and then cloning the gene into a plasmid vector. The plasmid vector containing the VSIG4 monoclonal antibody gene is transfected into the host cell using a suitable transfection method. The VSIG4 recombinant monoclonal antibody underwent affinity-chromatography purification. It is only reactive with the human species. Its specificity has been tested in ELISA. It can bind to the recombinant human VSIG4 protein (CSB-MP896869HU) with the EC₅₀ of 51.14-68.73 ng/mL.

The VSIG4 protein mainly regulates immune responses by interacting with immune cells such as T cells and macrophages. It is known to act as a co-stimulatory molecule, enhancing T cell activation, and also as an inhibitory molecule, suppressing the function of macrophages. VSIG4 has been shown to play a role in the regulation of autoimmune responses, tumor immunity, and infectious diseases. It is also involved in the clearance of apoptotic cells and the maintenance of tissue homeostasis.