The WNK1 recombinant monoclonal antibody is created using in vitro expression systems, which are established by cloning the DNA sequences of WNK1 antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human WNK1 protein. Subsequently, the genes encoding the WNK1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The WNK1 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA and IHC applications, demonstrating its reactivity with the human WNK1 protein.

WNK1 is a serine/threonine kinase that plays a central role in regulating ion transport, particularly sodium and potassium balance, in the kidneys. Its functions extend to blood pressure regulation, cell volume homeostasis, and potentially neuronal functions. Dysregulation of WNK1 can lead to electrolyte imbalances, hypertension, and other related disorders.

To create the mono/di/tri-methyl-histone H3.1 (K79) recombinant monoclonal antibody, the process initiates with the isolation of genes responsible for coding the HIST1H3A antibody from rabbits that have been previously exposed to a synthesized peptide originating from the human HIST1H3A protein methylated at K79. These antibody genes are then meticulously integrated into specialized expression vectors. Following this genetic modification, the vectors are thoughtfully introduced into host suspension cells, which are diligently cultivated to encourage the production and secretion of antibodies. After this cultivation phase, the mono/di/tri-methyl-histone H3.1 (K79) recombinant monoclonal antibody undergoes a rigorous purification process using affinity chromatography techniques, effectively separating the antibody from the surrounding cell culture supernatant. Finally, the functionality of the antibody is comprehensively assessed through ELISA, conclusively confirming its capability to interact effectively with the human HIST1H3A protein methylated at K79.

K79 methylation on HIST1H3A is often found at silenced or inactive gene loci. It marks these chromatin regions as transcriptionally inactive, preventing the binding of transcription factors and other regulatory proteins to the DNA. This leads to the repression of nearby genes. It is involved in proper chromosome organization and segregation during cell division.

In the production of the HRH3 recombinant monoclonal antibody, in vitro expression systems are utilized, entailing the cloning of HRH3 antibody DNA sequences from immunoreactive rabbits. The immunogen used in this process is a synthesized peptide derived from the human HRH3 protein. Subsequently, the genes encoding the HRH3 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. Following expression, the HRH3 recombinant monoclonal antibody is purified through affinity chromatography and subjected to extensive testing in ELISA and FC applications. These tests affirm the antibody's reactivity with the human HRH3 protein.

HRH3 protein, as a histamine receptor, plays a central role in modulating neurotransmitter release in the central nervous system. Its functions extend to regulating histamine levels, influencing cognitive processes, sleep-wake cycles, appetite, and various physiological and neuropsychiatric processes.

Through in vitro expression systems, the FDPS recombinant monoclonal antibody is synthesized by cloning the DNA sequences of FDPS antibodies sourced from immunoreactive rabbits. A synthesized peptide derived from the human FDPS protein serves as the immunogen in this process. The genes encoding the FDPS antibodies are subsequently inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells for antibody expression. After expression, the FDPS recombinant monoclonal antibody is subjected to affinity-chromatography purification. It is tested for functionality in ELISA and FC applications, demonstrating reactivity with the human FDPS protein during these assessments.

FDPS plays a central role in the biosynthesis of isoprenoids, with a primary focus on the production of farnesyl pyrophosphate (FPP). FPP is an essential precursor for various cellular processes, including the synthesis of sterols, protein prenylation, and the production of other isoprenoid compounds, all of which are critical for normal cell function and health. Dysregulation of this pathway can have significant implications for human health, including the development of metabolic and genetic disorders.

The DNA sequence coding for the histone H1.0 monoclonal antibody produced from the animals with human synthesized histone H1.0 peptide immunization was cloned into the expression vector, which was further transfected into a cell line for in vitro expression. The product is the recombinant histone H1.0 monoclonal antibody. It specifically targets the human histone H1.0. It belongs to the rabbit IgG. The affinity-chromatography purification method was used to purify this histone H1.0 antibody. This histone H1.0 can be used in ELISA.

Histone H1.0 is the most common variation at nucleoli-associated DNA domains (NADs), rDNA, and other repetitive sequences important in nucleolar structure. Histone H1.0 is a linker histone that plays a role in cell differentiation, stem cell maintenance, tumorigenesis, and extracellular vesicle (EV) formation, as well as affecting epigenetic and functional intra-tumor heterogeneity. H1.0 or its post-translational forms have also been discovered in EVs generated by cancer cells in culture, implying that these cells may avoid differentiation at least in part by discarding H1.0 via the EV route.

In the production of the KRT20 recombinant monoclonal antibody, in vitro expression systems are employed, involving the cloning of KRT20 antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human KRT20 protein. Subsequently, the genes encoding the KRT201 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. Post-expression, the KRT20 recombinant monoclonal antibody undergoes purification through affinity chromatography. It is thoroughly tested for functionality in ELISA, IHC, and FC applications, demonstrating reactivity with the human KRT20 protein during these evaluations.

The main role of KRT20 protein is to provide structural support and integrity to epithelial tissues, particularly in the gastrointestinal tract. KRT20 also serves as a tissue-specific marker and can be involved in diagnostic applications, especially in the context of certain types of cancers and pathological conditions affecting epithelial tissues.

The FPGS recombinant monoclonal antibody is generated through in vitro expression systems developed by cloning the DNA sequences of FPGS antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human FPGS protein. Subsequently, the genes encoding the FPGS antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The FPGS recombinant monoclonal antibody then undergoes affinity-chromatography purification and is rigorously tested for functionality in ELISA and FC applications. These tests confirm its reactivity with the human FPGS protein.

The main role of FPGS protein is to regulate and enhance the cellular uptake and utilization of folate by converting it into polyglutamate forms. This modification allows folate to be retained within cells, stored for future use, and optimally utilized in essential biochemical processes, including DNA synthesis, amino acid metabolism, and methylation reactions.

The process of producing the phospho-Histone H3.3 (T3) recombinant antibody commences with the cloning of the genes encoding the H3F3A antibody, encompassing both heavy and light chains, and their insertion into expression vectors. These modified vectors are then introduced into host cells through transfection, prompting the host cells to take on the role of antibody production and secretion. The resulting phospho-Histone H3.3 (T3) antibody is purified using affinity chromatography to ensure its purity and effectiveness. Rigorous testing follows to evaluate its functionality across a spectrum of applications, including ELISA, WB, ICC, and FC, all designed for the specific detection of the human and mouse H3F3A proteins phosphorylated at T3.

Phosphorylation of Histone H3.3 at threonine 3 (T3) is involved in transcriptional regulation, chromatin remodeling, DNA repair, cell cycle regulation, epigenetic signaling, and cellular memory, and has implications in various diseases. It is a dynamic modification that helps regulate gene expression and chromatin structure.

The production of the PXN recombinant monoclonal antibody relies on in vitro expression systems developed through the cloning of PXN antibody DNA sequences sourced from immunoreactive rabbits. The immunogen employed is a synthesized peptide derived from human paxillin. Subsequently, the PXN antibody genes are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. Following expression, the PXN recombinant monoclonal antibody is subjected to affinity-chromatography purification. It undergoes comprehensive testing in ELISA, IHC, and FC applications, confirming its reactivity with the human PXN protein.

Paxillin (PXN) is a versatile protein that plays a central role in cell adhesion, signaling, and cytoskeletal organization. Its functions are critical for various cellular processes, including cell adhesion, migration, and tissue development. Dysregulation of paxillin can have significant implications in diseases like cancer and neurological disorders.

The production of the di-methyl-Histone H3.1 (K4) recombinant monoclonal antibody is a meticulous process that initiates with the cloning of genes responsible for encoding the HIST1H3A antibody, encompassing both heavy and light chains. These cloned genes are then incorporated into expression vectors, which are subsequently introduced into host cells via transfection. The host cells are then tasked with producing and secreting the antibody. To ensure its purity and efficacy, the antibody undergoes a stringent purification process utilizing affinity chromatography. Following purification, the antibody is rigorously tested for functionality in a range of applications, including ELISA, WB, ICC, and IF, making it a versatile tool for accurately detecting the human and mouse HIST1H3A proteins di-methylated at K4.

Di-methylation of Histone H3.1 at lysine 4 (K4) primarily functions in transcriptional activation, chromatin accessibility, developmental regulation, epigenetic memory, coordinated gene regulation, and has implications in various diseases.