In the production of the BAX recombinant monoclonal antibody, in vitro expression systems are utilized, entailing the cloning of BAX antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human BAX protein. Subsequently, the genes encoding the BAX antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. Following expression, the BAX recombinant monoclonal antibody is purified through affinity chromatography and subjected to extensive testing in ELISA, IHC, and FC applications. These tests affirm its reactivity with the human BAX protein.
BAX is a critical regulator of apoptosis, promoting programmed cell death in response to various cellular signals and stressors. Its functions are essential for tissue homeostasis, the removal of damaged or unwanted cells, and the prevention of diseases such as cancer. BAX and other Bcl-2 family members help maintain the balance between cell survival and cell death in multicellular organisms.
In vitro expression systems are used to generate the PAX6 recombinant monoclonal antibody, involving the cloning of PAX6 antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human PAX6 protein. Subsequently, the genes encoding the PAX6 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. The PAX6 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA, IHC, and FC applications, confirming its reactivity with the human PAX6 protein.
PAX6 is a transcription factor that is crucial for the development of the eye, central nervous system, and other tissues. Its functions are essential for the formation and maintenance of various structures in the body, and its dysregulation can lead to developmental disorders and vision-related conditions.
To produce the phospho-MDM2 (S166) recombinant monoclonal antibody, in vitro expression systems are harnessed, involving the cloning of DNA sequences of MDM2 antibodies obtained from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human MDM2 protein that is phosphorylated at S166. Subsequently, the genes encoding the MDM2 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. Post-expression, the phospho-MDM2 (S166) recombinant monoclonal antibody undergoes affinity-chromatography purification and is extensively tested for functionality in ELISA, IHC, IF, and FC applications, confirming its reactivity with the human MDM2 protein phosphorylated at S166.
MDM2 is a critical regulator of the tumor suppressor protein p53. Phosphorylation at S166 reduces MDM2's ability to target p53 for degradation, allowing p53 to accumulate and execute its functions in response to cellular stress and DNA damage.
Employing in vitro expression systems, the KRT6A recombinant monoclonal antibody is synthesized by cloning DNA sequences of KRT6A antibodies sourced from immunoreactive rabbits. The immunogen utilized is a synthesized peptide derived from the human KRT6A protein. Subsequently, the genes coding for the KRT6A antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable the expression of the antibody. Following expression, the KRT6A recombinant monoclonal antibody undergoes affinity-chromatography purification and is rigorously tested for functionality in ELISA, IF, and FC applications, confirming reactivity with the human KRT6A protein.
KRT6A is a keratin protein that primarily provides structural support to epithelial tissues, including the skin, hair, and nails. Its functions are essential for maintaining the structural integrity of these tissues and for protecting the body from external factors. Dysregulation of KRT6A and other keratins can lead to various skin and nail disorders.
To manufacture the mono-methyl-histone H2B type 2-E (R79) recombinant monoclonal antibody, the journey begins with the retrieval of genes responsible for encoding the HIST2H2BE antibody from rabbits that have previously undergone immunization with a synthesized peptide originating from the human HIST2H2BE protein mono-methylated at R79. Subsequently, these antibody genes are seamlessly 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 growth phase, the mono-methyl-histone H2B type 2-E (R79) recombinant monoclonal antibody undergoes a meticulous purification process using affinity chromatography techniques, effectively isolating the antibody from the surrounding cell culture supernatant. Lastly, the functionality of the antibody is rigorously assessed through ELISA, conclusively affirming its ability to effectively react with the human HIST2H2BE protein mono-methylated at R79.
The PITX3 recombinant monoclonal antibody is synthesized through in vitro expression systems that involve cloning the DNA sequences of PITX3 antibodies from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human PITX3 protein. Following this, the genes encoding the PITX3 antibodies are incorporated into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. Upon expression, the PITX3 recombinant monoclonal antibody undergoes purification through affinity chromatography. Rigorous testing in ELISA, IF, and FC applications confirms the antibody's reactivity with the human PITX3 protein.
The main role of the PITX3 protein is to function as a transcription factor that regulates the development and maintenance of various components of the eye, including the lens, cornea, and ciliary body. Its proper functioning is essential for normal eye development and vision, and mutations in the PITX3 gene can lead to congenital cataracts and other eye-related disorders.
CUSABIO produced the CD20 monoclonal antibody by immunizing animals with a synthesized peptide deduced from human CD20. The vector engineered by inserting the DNA sequence encoding CD20 monoclonal antibody was transfected into the cell line for expression. The product was affinity-chromatography purified and got the CD20 recombinant monoclonal antibody. It is a rabbit IgG. This CD20 antibody can be used to detect the human CD20 in ELISA.
CD20 is a B cell differentiation antigen that is widely expressed from early pre-B to mature B cell stages but is eliminated as B cells differentiate into plasma cells. Anti-CD20 monoclonal antibodies including rituximab, ofatumumab, and obinutuzumab have improved the treatment of B-cell malignancies.
CD45 antibody CSB-RA019049A0HU is a recombinant monoclonal antibody produced from the expression of the plasmids that were constructed by the CD45 monoclonal antibody (generated from animals with the human CD45 synthesized peptide immunization) DNA sequence in cell lines. The CD45 antibody was purified through the affinity-chromatography method. It is a rabbit IgG antibody. It reacts with the CD45 protein from human samples. And it is suitable for ELISA analysis.
CD45 is a receptor-like tyrosine phosphatase that is only found in the hematopoietic system. CD45 plays a crucial function in the growth and activation of T lymphocytes. CD45 is a valuable marker for the differential diagnosis of undifferentiated lymphoma because of its leukocyte-specific tissue distribution.