The production of the GAPDH recombinant monoclonal antibody involves acquiring the GAPDH antibody genes, introducing these genes into suitable host cells, and employing a cellular expression and translation system to manufacture GAPDH antibodies. This approach offers several benefits, including a substantial enhancement in the purity and stability of the synthesized GAPDH recombinant monoclonal antibodies, along with improvements in antibody affinity and specificity. After synthesis, the GAPDH recombinant monoclonal antibody undergoes purification through affinity chromatography and undergoes extensive testing, including ELISA, WB, IHC, IF, and FC assays. Importantly, this antibody specifically targets the human GAPDH protein.

GAPDH's primary role is in glycolysis, where it participates in energy production and NADH generation. It also has diverse functions in cellular regulation, redox signaling, apoptosis, and RNA metabolism.

The phospho-AKT1 (Ser473) recombinant monoclonal antibody is prepared through a combination of protein technology and DNA recombinant techniques. To begin, mice are immunized with a synthesized peptide derived from human phospho-AKT1 (Ser473), stimulating the production of B cells. Positive B cells are then selected and perform single clone identification. The resulting genes encoding the phospho-AKT1 (Ser473) antibody are amplified through PCR and inserted into a plasmid vector, creating a recombinant vector. This recombinant vector is introduced into host cells for antibody expression. The phospho-AKT1 (Ser473) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It has been tested for use in five applications, including ELISA, WB, IHC, IF, and IP, and can react with human AKT1 protein phosphorylated at Ser473 residue.

In the process of creating the phospho-PRKAA2 (S491) recombinant monoclonal antibody, the initial step involves the isolation of genes responsible for encoding the PRKAA2 antibody from rabbits that have been immunized with a synthesized peptide derived from the human PRKAA2 protein phosphorylated at S491. Subsequently, these antibody genes are cloned into expression vectors. Following this genetic modification, the modified vectors are carefully transfected into host suspension cells. Once transfection is successful, positive cells are cultivated to facilitate the expression and secretion of antibodies. The phospho-PRKAA2 (S491) recombinant monoclonal antibody is then purified from the cell culture supernatant using affinity chromatography. Finally, the antibody's activity is rigorously assessed through ELISA and WB tests, confirming its capability to interact effectively with the human PRKAA2 protein phosphorylated at S491.

Phosphorylation of PRKAA2 at S491 is a crucial regulatory event in the AMPK signaling pathway, allowing cells to adapt to energy fluctuations and maintain energy homeostasis. Dysregulation of this phosphorylation event can have significant implications for cellular metabolism and is implicated in various metabolic disorders and cancers.

To produce the phospho-MAPT (S324) recombinant monoclonal antibody, the initial step involves isolating the genes responsible for coding the MAPT antibody from rabbits that have been immunized with a synthesized peptide derived from the human MAPT protein phosphorylated at S324. These antibody genes are then cloned into specialized expression vectors. Following this genetic modification, the vectors are introduced into host suspension cells. Subsequently, positive cells are cultured to facilitate the expression and secretion of antibodies. The phospho-MAPT (S324) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. Finally, the antibody's functionality is rigorously tested through ELISA and IF assays, confirming its ability to react with human MAPT protein phosphorylated at S324.

The production of the recombinant monoclonal antibody targeting PTPRC entails the initial step of introducing PTPRC antibody genes into plasmid vectors. These engineered plasmids are subsequently introduced into suitable host cells for expression using exogenous protein expression technology. Following this, the PTPRC recombinant monoclonal antibody undergoes a purification process using affinity chromatography. It has undergone rigorous validation for specific applications, including ELISA and FC. Importantly, this antibody exclusively recognizes the human PTPRC protein.

PTPRC (CD45) is a critical regulator of immune cell activation and signaling. It fine-tunes immune responses by modulating the phosphorylation status of key signaling molecules, ensuring proper immune cell development, antigen recognition, activation, and immune response regulation. Dysregulation of PTPRC can lead to immune disorders and impaired immune function.

The production of the recombinant monoclonal antibody specific to SNCA involves initially inserting SNCA antibody genes into plasmid vectors. These engineered plasmid vectors are subsequently introduced into appropriate host cells for expression. Afterward, the SNCA recombinant monoclonal antibody undergoes purification using affinity chromatography. It has undergone thorough validation for various applications, including ELISA, IHC, IF, and FC. This antibody exclusively recognizes the human SNCA protein.

SNCA is predominantly found in neurons, particularly in the presynaptic terminals, where it participates in several important processes, including regulation of synaptic vesicles, maintenance of synaptic integrity, neuronal plasticity, dopamine regulation, formation of Lewy Bodies, and cellular stress response.

In the process of generating the phospho-MAPK8/MAPK9/MAPK10 (T183/T183/T221) recombinant monoclonal antibody, the initial step involves the isolation of genes responsible for encoding the MAPK8/MAPK9/MAPK10 (T183/T183/T221) antibody. These genes are sourced from rabbits that have been previously immunized with a synthesized peptide derived from the human phospho-MAPK8/MAPK9/MAPK10 (T183/T183/T221) protein. Subsequently, these antibody genes are cloned into specialized expression vectors. Following this genetic modification, the vectors are skillfully introduced into mammalian suspension cells. These mammalian cells are then cultured, providing an environment conducive to the production and secretion of the antibodies. Moving forward, the phospho-MAPK8/MAPK9/MAPK10 (T183/T183/T221) recombinant monoclonal antibody undergoes a meticulous purification process that hinges on the principles of affinity chromatography, effectively separating the antibody from the surrounding cell culture supernatant. Lastly, the antibody's functionality is subjected to a comprehensive evaluation, spanning a diverse array of tests including ELISA, WB, and IHC, thereby confirming its capability to effectively interact with the human phospho-MAPK8/MAPK9/MAPK10 (T183/T183/T221) protein.

To produce the HMGB1 recombinant monoclonal antibody, the HMGB1 antibody genes were integrated into plasmid vectors. These engineered plasmid vectors were subsequently introduced into appropriate host cells using exogenous protein expression techniques, facilitating antibody production. Following this production phase, the HMGB1 recombinant monoclonal antibody underwent purification via affinity chromatography. Rigorous validation was carried out to confirm the suitability of this HMGB1 recombinant monoclonal antibody for various applications, including ELISA, IHC, and FC.

HMGB1 is a nuclear protein that can be released from cells and act as an extracellular signaling molecule. HMGB1 protein has diverse functions, including its role in DNA binding, chromatin organization, inflammation, immunity, cell survival, tissue repair, cancer, and neuronal function.

In the development of the phospho-TP53 (S9) recombinant monoclonal antibody, the initial phase involves the retrieval of genes encoding the TP53 antibody from rabbits immunized with a synthetic peptide originating from the human TP53 protein phosphorylated at S9. Following this, these genes are adeptly integrated into expression vectors. Subsequently, these genetically modified vectors are introduced into mammalian suspension cells, where they are thoughtfully cultivated to encourage the production and secretion of the antibodies. Following this growth phase, an intricate purification process employing affinity chromatography is executed to meticulously isolate the phospho-TP53 (S9) recombinant monoclonal antibody from the surrounding cell culture supernatant. Lastly, the functionality of the antibody is meticulously scrutinized through ELISA and IF tests, conclusively affirming its capacity to engage with the human TP53 protein phosphorylated at S9.

Phosphorylation of p53 at S9 serves as a crucial regulatory mechanism to maintain genomic integrity and prevent the development of cancer by coordinating DNA repair, cell cycle control, and cell fate decisions in response to stress and damage. Dysregulation of p53 phosphorylation can lead to uncontrolled cell proliferation and is often observed in cancer cells.

To produce the CD69 recombinant monoclonal antibody, the CD69 antibody genes were first incorporated into plasmid vectors. These engineered plasmid vectors were subsequently introduced into suitable host cells using exogenous protein expression techniques to facilitate antibody production. After this production step, the CD69 recombinant monoclonal antibody underwent purification via affinity chromatography. This CD69 recombinant monoclonal antibody was validated for ELISA. In the functional ELISA, it was demonstrated that the CD69 recombinant monoclonal antibody effectively bound to the human CD69 protein (CSB-MP004952HU) at a concentration of 2 μg/mL, with an EC₅₀ ranging from 23.17 to 26.04 ng/mL.

CD69 is a surface protein found on immune cells, particularly T cells and NK cells, and its main function is to serve as an early activation marker. It plays a role in immune cell retention, immune regulation, signal transduction, and tissue-specific functions.