The generation of the CD44 recombinant monoclonal antibody relies on in vitro expression systems, which are established by cloning the DNA sequences of CD44 antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human CD44 protein. Subsequently, the genes encoding the CD44 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to facilitate antibody expression. Following expression, the CD44 recombinant monoclonal antibody undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA, WB, IHC, IF, and FC applications, confirming its reactivity with the human CD44 protein.

CD44 is a versatile cell surface glycoprotein with numerous functions in cell adhesion, migration, signaling, and immune responses. Its roles extend to various physiological processes and pathological conditions, including inflammation, cancer, tissue development, and stem cell regulation.

Through the utilization of in vitro expression systems, the ASS1 recombinant monoclonal antibody is synthesized by cloning DNA sequences of ASS1 antibodies sourced from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human ASS1 protein. Subsequently, the genes encoding the ASS1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. The ASS1 recombinant monoclonal antibody undergoes affinity-chromatography purification and is rigorously tested for functionality in ELISA, IHC, IF, and FC applications, displaying reactivity with the human ASS1 protein during these assessments.

The primary function of the ASS1 protein is to participate in the urea cycle and arginine synthesis. ASS1 plays a crucial role in detoxifying ammonia, synthesizing arginine, and maintaining nitrogen balance in the body. Dysregulation or deficiency of ASS1 can lead to metabolic disorders associated with ammonia toxicity and arginine deficiency.

Through in vitro expression systems, the LEF1 recombinant monoclonal antibody is synthesized by cloning the DNA sequences of LEF1 antibodies sourced from immunoreactive rabbits. A synthesized peptide derived from the human LEF1 protein serves as the immunogen in this process. The genes encoding the LEF1 antibodies are subsequently inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells for antibody expression. After expression, the LEF1 recombinant monoclonal antibody is subjected to affinity-chromatography purification and is extensively tested for functionality in ELISA and IHC applications, demonstrating reactivity with the human LEF1 protein during these assessments.

LEF1 is a transcription factor with diverse functions in various biological processes, including embryonic development, tissue homeostasis, cell differentiation, and cancer. Its role as a key mediator of the Wnt signaling pathway makes it a critical regulator of gene expression and cellular responses to Wnt ligands, ultimately influencing tissue development and maintenance.

The DYNLL1 recombinant monoclonal antibody is synthesized through in vitro expression systems developed by cloning the DNA sequences of DYNLL1 antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human DYNLL1 protein. Subsequently, the genes encoding the DYNLL1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The DYNLL1 recombinant monoclonal antibody is then subjected to affinity-chromatography purification, followed by rigorous testing in ELISA, IHC, and FC applications, confirming its reactivity with the human DYNLL1 protein.

DYNLL1 is a regulatory protein that plays a central role in intracellular transport by interacting with dynein motors. Its functions extend to various cellular processes, including intracellular transport, mitosis, neuronal axonal transport, cellular organization, and cellular motility. Proper regulation of DYNLL1 is essential for maintaining normal cellular structure and function.

The SLC7A11 recombinant monoclonal antibody is obtained by constructing the SLC7A11 antibody genes into plasmid vectors and then transfecting the constructed plasmid vectors into suitable host cells for expression through exogenous protein expression technology. This SLC7A11 recombinant monoclonal antibody underwent affinity-chromatography purification and was validated for ELISA. In the functional ELISA, the human SLC7A11 protein (CSB-CF892171HU(A4)) at 2 μg/mL can bind this SLC7A11 recombinant monoclonal antibody, with the EC₅₀of 9.452-13.79 ng/mL.

SLC7A11 is a component of a heterodimeric amino acid transporter known as system xCT, which consists of SLC7A11 and SLC3A2. SLC7A11 functions as the light chain subunit of this transporter. The primary role of SLC7A11 is to exchange cystine for glutamate, across the cell membrane. It also regulates redox balance.

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

NANOG protein plays a crucial role in regulating pluripotency and self-renewal in stem cells, particularly in ESCs and iPSCs. Its functions are essential for early embryonic development, stem cell maintenance, and cell fate determination.

The PAX8 recombinant monoclonal antibody is produced through in vitro expression systems, involving the cloning of PAX8 antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human PAX8 protein. Subsequently, the genes encoding the PAX8 antibodies are incorporated into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. The PAX8 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is extensively tested for functionality in ELISA and IHC applications, displaying reactivity with the human PAX8 protein during these assessments.

PAX8 is a transcription factor that is critical for the development and function of various tissues and organs, including the thyroid gland, kidneys, female reproductive system, and potentially other tissues. Its role in regulating gene expression is essential for tissue differentiation, development, and function.

The process of generating the mono/di/tri-methyl-histone H3.1 (K14) recombinant antibody starts with the cloning of genes encoding the HIST1H3A antibody, encompassing both heavy and light chains. These cloned genes are then incorporated into expression vectors, which are introduced into host cells via transfection. The host cells are responsible for producing and secreting the antibody. Following purification using affinity chromatography to ensure its purity, the antibody undergoes stringent functionality testing through ELISA, facilitating accurate detection of the human HIST1H3A protein mono/di/tri-methylated at K14.

H3.1 mono-methylation at K14 is associated with both transcriptional activation and repression, depending on the context. Di- or tri-methylation at H3.1 K14 is often linked to transcriptional repression. Di-methylation at H3.1 K14 can be involved in the regulation of genes associated with development, differentiation, and cell cycle control. Tri-methylation at H3.1 K14 is involved in the regulation of genes important for cellular identity, development, and genome stability.

The SCGB1A1 recombinant monoclonal antibody is generated through in vitro expression systems, involving the cloning of SCGB1A1 antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human SCGB1A1 protein. Subsequently, the genes encoding the SCGB1A1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The SCGB1A1 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA and FC applications, displaying reactivity with the human SCGB1A1 protein during these evaluations.

SCGB1A1, also known as Clara cell secretory protein (CCSP), is a protein primarily produced by Clara cells in the respiratory tract, and its main functions are to protect the lungs from oxidative stress, inflammation, and pathogens, while also contributing to lung homeostasis and repair.