The phospho-EGFR (Y1068) recombinant monoclonal antibody is yielded through the implementation of protein technology and DNA recombinant techniques. Initially, animals are immunized with a synthesized peptide derived from human phospho-EGFR (Y1068). Next, B cells are obtained from the mice. Through a screening process, positive B cells are selected and undergo single clone identification. The light and heavy chains of the phospho-EGFR (Y1068) antibody are then amplified via PCR and inserted into a plasmid vector, creating a recombinant vector, which is transfected into host cells for the expression of the antibody. Subsequently, the phospho-EGFR (Y1068) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It is recommended for use in ELISA and WB for the detection of human EGFR phosphorylated at Y1068 residue.

To produce a recombinant monoclonal antibody against BCL6, CUSABIO initiated the process by immunizing a rabbit with a synthesized peptide derived from human BCL6 protein. Following immunization, B cells were isolated from the rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was used as a template to extend BCL6 antibody genes using degenerate primers. These extended BCL6 antibody genes were then incorporated into a plasmid vector and transfected into host cells for expression. Subsequently, the BCL6 recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and evaluated for its suitability in ELISA, IHC, and FC applications, demonstrating specific recognition of human BCL6 protein.

BCL6 is a critical transcriptional repressor that regulates B cell development, germinal center formation, and the adaptive immune response. Its functions are essential for generating high-affinity antibodies and maintaining the balance between immune response and immune tolerance. Dysregulation of BCL6 can have significant implications for B cell lymphomagenesis and immune-related diseases.

CUSABIO designed the vector clones for the expression of a recombinant RAF1 antibody in mammalian cells. The vector clones were obtained by inserting the RAF1 antibody heavy and light chains into the plasma vectors. The recombinant RAF1 antibody was purified from the culture medium through affinity-chromatography. It can be used to detect RAF1 protein from Human in the ELISA, WB, IF.

RAF1 is a kinase that acts as the effector associating RAS with MEK/ERK activation. It is involved in multiple cellular activities such as cell proliferation, differentiation, cell death and survival, metabolism, and motility. RAF1 is essential for the development of skin and lung tumors and can negatively regulate hepatocarcinogenesis. RAF1 is regulated by phosphorylation, and phosphorylation at the S621 enhances RAF1 kinase activity by providing a second, positive binding site for 14-3-3, which is required for RAF1 kinase activity.

The rabbit was immunized with a synthesized peptide from the human CLDN5 protein. Subsequently, B cells were isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was then reverse-transcribed into cDNA, serving as a template for extending CLDN5 antibody genes using degenerate primers. The resulting CLDN5 antibody genes were incorporated into a plasmid vector, followed by transfection into host cells for expression. The resulting CLDN5 recombinant monoclonal antibody was purified from the cell culture supernatant using affinity chromatography. The CLDN5 antibody was assessed for its utility in ELISA and IHC applications, with the ability to recognize human CLDN5 protein.

The CLDN5 protein, as a component of tight junctions, plays a central role in regulating the permeability of endothelial barriers, particularly in the formation and maintenance of the blood-brain barrier. Its functions are crucial for preserving tissue homeostasis and protecting the brain from potential threats.

To create the phospho-RAF1 (S259) recombinant monoclonal antibody, the first step involves obtaining the genes responsible for coding this RAF1 antibody. These genes are sourced from rabbits previously exposed to a synthesized peptide derived from the human RAF1 protein phosphorylated at S259. Subsequently, these antibody genes are cloned into specialized expression vectors. Following this genetic modification, the vectors are carefully transfected into host suspension cells, which are then diligently cultivated to promote the expression and secretion of antibodies. The phospho-RAF1 (S259) recombinant monoclonal antibody is then subjected to a meticulous purification process using affinity chromatography, effectively separating the antibody from the surrounding cell culture supernatant. Finally, the antibody's functionality is rigorously assessed through a battery of tests, including ELISA, WB, IHC, and IF, confirming its capability to effectively interact with the human RAF1 protein phosphorylated at S259.

Phosphorylation of RAF1 at S259 is a critical regulatory event in the MAPK signaling pathway, helping to control cell proliferation, differentiation, and survival. Dysregulation of this phosphorylation event can have significant implications for cancer and other diseases driven by abnormal signaling pathways.

Immunizing the rabbit with the synthesized peptide derived from human GRIN1 protein and then isolating B cells from the immunized rabbit, followed by extracting RNA from the B cells. The extracted RNA was reversely transcribed into cDNA, which acted as the template to extend GRIN1 antibody genes with degenerate primer. The synthesized GRIN1 antibody genes were inserted into the plasmid vector and then transfected into host cells for expression. The GRIN1 recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography. It was subjected to ELISA and FC applications. It can react with human GRIN1 protein.

The GRIN1 protein, as a subunit of the NMDA receptor, is central to various essential processes in the nervous system, including synaptic plasticity, learning, memory, and normal neurotransmission. Dysregulation of NMDA receptors can have significant implications for neurological health and disorders.

The vectors expressing anti-MTOR antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-MTOR (S2481), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening MTOR antibody gene, and amplifying heavy and light chain sequence by PCR and cloning them into plasma vectors. After that, the vector clones were transfected into the mammalian cells for production. The product is the recombinant MTOR antibody. Recombinant MTOR antibody in the culture medium was purified using affinity-chromatography. It can react with MTOR protein from Human and is used in the ELISA, WB, IF.

The protein encoded by mTOR belongs to the phosphatidylinositol kinase-related kinase family. These kinases mediate cellular responses to stress, such as DNA damage and nutrient starvation. According to some studies, MTOR may have the following features.
mTOR has come a long way from its humble beginnings as a kinase of unknown function. As part of the mTORC1 and mTORC2 complexes, mTOR plays a pivotal role in several pathways involved in human cancer, sparking interest in mTOR inhibitors and placing them in the focus of the pharmaceutical industry. mTOR, a large protein kinase, is also the target of rapamycin, an immunosuppressant that also blocks vascular restenosis and has potential anticancer effects. mTOR interacts with Raptor and GβL proteins 1, 2, and 3 to form a complex that is the target of rapamycin.

The production of the FCGR3A recombinant monoclonal antibody initiates with the acquisition of FCGR3A antibody genes. These genes are then introduced into suitable host cells, which are cultured for synthesizing FCGR3A antibodies using a cell-based expression and translation system. This approach offers numerous advantages, including a substantial improvement in the purity and stability of the resultant FCGR3A recombinant monoclonal antibodies, along with enhancements in antibody affinity and specificity. Subsequent to synthesis, the FCGR3A recombinant monoclonal antibody undergoes purification via affinity chromatography. It is recommended for use in ELISA and IF. This antibody exclusively targets the human FCGR3A protein.

FCGR3A is an important receptor involved in the recognition and response to antibodies, particularly in ADCC and phagocytosis. Its activation on immune cells is a key mechanism for targeting and eliminating infected or abnormal cells and pathogens, contributing to the body's defense against infections and cancer.

The production of the recombinant monoclonal antibody targeting FTH1 involves a series of steps. Firstly, FTH1 antibody genes are incorporated into plasmid vectors. These modified plasmid vectors are then introduced into suitable host cells for expression using exogenous protein expression technology. Following this, the FTH1 recombinant monoclonal antibody undergoes purification via affinity chromatography. It has undergone thorough validation for specific applications, including ELISA, WB, IHC, and FC. It's important to note that this antibody binds to both human and mouse FTH1 proteins.

FTH1 is a critical protein involved in iron homeostasis within cells. It functions as an iron-storage protein, helping store excess iron and release it when needed for cellular processes. Proper regulation of FTH1 and ferritin complexes is essential for maintaining iron balance and preventing iron-related toxicity.

To create the recombinant monoclonal antibody directed against CD19, the first step involves the incorporation of CD19 antibody genes into plasmid vectors. These modified plasmid vectors are then introduced into suitable host cells for expression using exogenous protein expression technology. Following this, the CD19 recombinant monoclonal antibody undergoes purification using affinity chromatography. It has undergone rigorous validation for specific applications, including ELISA and WB. It is essential to note that this antibody binds to both human and mouse CD19 proteins.

CD19 protein is a key co-receptor on the surface of B cells that plays a central role in B cell activation, differentiation, and regulation of the adaptive immune response. Its functions are critical for mounting effective immune responses to pathogens and maintaining immune system balance.