The SLC2A2 recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, SLC2A2 antibody genes are extracted from B cells isolated from immunoreactive rabbits. These genes undergo amplification and are cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies in significant quantities. The resulting SLC2A2 recombinant monoclonal antibody undergoes affinity chromatography purification. It can be used to detect human SLC2A2 protein in ELISA, IHC, IF, and FC applications.

SLC2A2 is a vital transporter protein that helps regulate blood glucose levels and plays a central role in glucose metabolism, making it essential for overall metabolic health and diabetes management.

The RELA recombinant monoclonal antibody is synthesized in vitro through a systematic process. Initially, RELA antibody genes are isolated from B cells derived from immunoreactive rabbits. These genes undergo amplification and are cloned into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the generation of functional antibodies in significant quantities. The resulting RELA recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It is well-suited for various applications, including ELISA, WB, IF, and FC, enabling the specific detection of human RELA protein.

RELA is a critical component of the NF-κB complex that serves as a central regulator of immune responses, inflammation, and various cellular processes. Dysregulation of RELA activity can contribute to a range of diseases, including autoimmune disorders, inflammatory conditions, and cancer.

The FLT1 recombinant monoclonal antibody is generated through in vitro processes using synthetic genes. This methodology involves the retrieval of FLT1 antibody genes from B cells sourced from immunoreactive rabbits, followed by their amplification and cloning into appropriate phage vectors. These vectors are then introduced into mammalian cell lines, enabling the production of functional antibodies in substantial quantities. Subsequently, the FLT1 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It is well-suited for a wide range of applications, including ELISA, WB, IHC, and FC, facilitating the precise detection of human and mouse FLT1 proteins.

FLT1, also known as VEGFR-1, is to serve as a receptor for VEGF and PlGF. Upon binding to its ligands, FLT1 initiates intracellular signaling pathways that are crucial for angiogenesis, the process of forming new blood vessels. By transducing these signals, FLT1 plays a pivotal role in regulating vascular development, endothelial cell proliferation, migration, and survival, ultimately influencing processes like wound healing, embryonic development, and pathological conditions such as tumor angiogenesis.

The production of the TMEFF2 monoclonal antibody involved using the recombinant human TMEFF2 protein as the immunogen. The cDNA of the TMEFF2 monoclonal antibody was sequenced and obtained the TMEFF2 monoclonal antibody gene, which was then cloned into a plasmid vector. The plasmid vector carrying the TMEFF2 monoclonal antibody gene was transfected into the host cell using a suitable transfection method. The resulting TMEFF2 recombinant monoclonal antibody was then subjected to affinity-chromatography purification. Its specificity was confirmed through ELISA, where it showed binding to the recombinant human TMEFF2 (CSB-MP883439HU) with an EC₅₀ range of 2.129-2.956 ng/mL. It can react with TMEFF2 protein.

TMEFF2 is expressed in several tissues, including the brain, lung, prostate, and breast. TMEFF2 mainly functions as a tumor suppressor, as it has been shown to inhibit cell proliferation and induce apoptosis in certain types of cancer cells, including prostate and breast cancer. TMEFF2 has also been suggested to have a role in neuronal differentiation and migration during brain development, and may be involved in the regulation of synaptic transmission.

The production of the IL12&IL23 recombinant monoclonal antibody involves several steps: separating B cells from the spleen of the immunized animal and using recombinant human IL12&IL23 protein as the immunogen during the immunization process. RNA was isolated from the B cells and converted into cDNA. With the cDNA as the template, the IL12&IL23 antibody-encoding gene was amplified through PCR and cloned into the vector. The recombinant vector was transfected into host cells for antibody expression. The IL12&IL23 recombinant monoclonal antibody was harvested from the cell culture supernatant and purified using affinity chromatography. The antibody was validated by demonstrating its reactivity with human IL12 and IL23 proteins in ELISA.

CUSABIO produced the TPBG recombinant monoclonal antibody through a series of steps. Firstly, B cells were obtained from the spleen of the immunized animal, where the recombinant human TPBG protein served as the immunogen during the immunization process. RNA was then isolated from the B cells and converted into cDNA through reverse transcription. Using the cDNA as a template, the gene encoding the TPBG antibody was extended with a degenerate primer and then inserted into a recombinant vector. The vector was introduced into host cells via transfection to enable antibody expression. The TPBG recombinant monoclonal antibody was harvested from the cell culture supernatant and purified using affinity chromatography. To validate the antibody, it underwent testing for reactivity with human and macaca mulatta TPBG proteins in ELISA, confirming its specificity and functionality.

CUSABIO developed the CLDN3 recombinant monoclonal antibody using a multi-step process. Initially, B cells were isolated from the spleen of the immunized animal, with the recombinant human CLDN3 protein employed as the immunogen during immunization. Subsequently, RNA was extracted from the B cells and converted into cDNA through reverse transcription. The gene encoding the CLDN3 antibody was extended using a degenerate primer through PCR and inserted into the vector. The recombinant vector was introduced into host cells via transfection, facilitating antibody expression. The CLDN3 recombinant monoclonal antibodies were obtained from the cell culture supernatant and purified using affinity chromatography. To confirm specificity and functionality, this antibody was validated through ELISA, demonstrating its ability to react with human CLDN3 protein.

CUSABIO undertook a stepwise approach to produce the CEACAM5/CEACAM6 recombinant monoclonal antibody. Initially, B cells were isolated from the spleen of an immunized animal, utilizing recombinant human CEACAM5/CEACAM6 protein as the immunogen during the immunization process. Subsequently, RNA was extracted from the B cells and reversely transcribed into cDNA. Using the cDNA as a template, the gene encoding the CEACAM5/CEACAM6 antibody was extended with a degenerate primer and inserted into a vector. This recombinant vector was then transfected into host cells to enable antibody expression. The CEACAM5/CEACAM6 recombinant monoclonal antibodies were harvested from the cell culture supernatant and purified via affinity chromatography. To validate this antibody's specificity, it underwent testing in ELISA to confirm its reactivity with human CEACAM5 and CEACAM6 proteins.

The process for generating the mono-methyl-HIST1H3A (K9) recombinant monoclonal antibody typically begins with the incorporation of the HIST1H3A antibody-encoding gene into expression vectors. These vectors are then transferred into host cells via polyethyleneimine-mediated transfection methods. 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, IHC, IF, and FC assays, demonstrating their specific binding to the human HIST1H3A protein mono-methylated at K9.

HIST1H3A mono-methylated at K9 is typically found in regions of the genome associated with heterochromatin and plays a central role in epigenetic regulation by contributing to gene repression and the formation of transcriptionally silent heterochromatin. This modification is crucial for maintaining proper gene expression patterns and cellular identity and has implications for various biological processes and disease states.

The acetyl-HIST1H3A recombinant monoclonal antibody expression typically involves the initial step of inserting the HIST1H3A antibody-encoding gene into expression vectors. These vectors are then delivered into host cells via 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, IF, and FC tests, confirming their capacity to recognize the human acetylated HIST1H3A protein.

Acetylated HIST1H3A serves as a key epigenetic mark associated with the activation of gene expression. It modulates chromatin structure, making genes more accessible for transcription. This process plays crucial roles in various cellular processes, including development, differentiation, and the response to environmental cues.