The CLDN6/9 recombinant monoclonal antibody was meticulously produced by CUSABIO following a well-defined process. B cells were isolated from the spleen of an immunized animal, with the recombinant human CLDN6/9 protein used as the immunogen during the immunization procedure. RNA was extracted from the B cells and reverse-transcribed into cDNA. The gene encoding the CLDN6/9 antibody was then extended using a degenerate primer and inserted into a vector. This recombinant vector was subsequently introduced into host cells through transfection, enabling efficient antibody expression. The CLDN6/9 recombinant monoclonal antibodies were harvested from the cell culture supernatant and purified using affinity chromatography. Extensive validation, including ELISA and FC testings, was conducted to confirm this antibody's reactivity with human CLDN6 and CLDN9 protein, ensuring its accuracy and suitability for further applications.

The SIRPA recombinant monoclonal antibody synthesis starts with the extraction of SIRPA antibody genes from B cells that are 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. The resulting SIRPA recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. After rigorous verification, the antibody can be used in ELISA, IHC, and FC applications to detect the human SIRPA protein.

SIRPA is a protein that regulates immune responses and phagocytosis by interacting with CD47 and other ligands. Its main function is to prevent the unnecessary phagocytosis of healthy cells while facilitating the clearance of pathogens and damaged cells by immune cells. SIRPA's role in immune regulation has implications for both normal immune function and potential therapeutic strategies for cancer and other diseases.

The GLA recombinant monoclonal antibody is synthesized in vitro through a systematic process. Initially, GLA 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. The resulting GLA recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It shows reactivity with human GLA protein and can be used in ELISA, IHC, and FC applications.

GLA is primarily active in lysosomes, cellular organelles responsible for breaking down various molecules. Alpha-galactosidase A (GLA) mainly catalyzes the hydrolysis of the alpha-galactosides. This enzyme plays a crucial role in the breakdown of complex carbohydrates in the body, particularly a substrate known as globotriaosylceramide (Gb3), also called ceramide trihexoside.

The LCP1 recombinant monoclonal antibody is generated through in vitro processes using synthetic genes. The LCP1 antibody genes are first isolated from B cells that are sourced from immunoreactive rabbits, followed by their amplification and cloning into appropriate phage vectors. These vectors are then transfected into mammalian cell lines, enabling the production of functional antibodies. Subsequently, the LCP1 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. This antibody shows good results in the detection of human LCP1 protein in ELISA and FC applications.

LCP1 is an actin-binding protein that plays a crucial role in the organization and regulation of the actin cytoskeleton. Its functions are diverse and include influencing cell migration, immune cell activation, microvilli formation, cancer metastasis, neuronal processes, and the regulation of immune responses. Its ability to crosslink actin filaments contributes to cellular structure and function in a variety of cell types.

The GAA recombinant monoclonal antibody is synthetically generated in vitro, starting with the extraction of GAA antibody genes from B cells isolated from immunoreactive rabbits. These GAA antibody genes are then amplified and cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to enable the production of functional antibodies. Following this, the GAA recombinant monoclonal antibody undergoes affinity chromatography purification. This antibody shows good results in the detection of human GAA protein in ELISA and IHC applications.

Lysosomal alpha-glucosidase (GAA) is a crucial enzyme involved in the breakdown of glycogen within lysosomes. Its primary function is to hydrolyze glycogen into glucose, helping to maintain glucose homeostasis and prevent glycogen accumulation in various tissues. Dysfunction or deficiency of this enzyme can lead to serious health conditions, such as Pompe disease.

The TNNT2 recombinant monoclonal antibody generation is a multi-step in vitro process. Initially, TNNT2 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. The resulting TNNT2 recombinant monoclonal antibody is purified through affinity chromatography. It can be used to detect human TNNT2 protein in ELISA, IHC, and FC applications.

TNNT2 is a critical protein in cardiac muscle, where it regulates muscle contraction and relaxation by sensing changes in intracellular calcium levels. Its role in the troponin complex ensures proper heart function and the efficient pumping of blood throughout the circulatory system.

The BDNF recombinant monoclonal antibody is synthesized in vitro through a systematic process. The BDNF antibody genes are first isolated from B cells derived from immunoreactive rabbits. Then, 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. The resulting BDNF recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. This antibody shows good results in the detection of human and mouse BDNF proteins in ELISA and WB applications.

BDNF is a crucial neurotrophic factor that supports the growth, survival, and plasticity of neurons. Its functions extend to various aspects of brain health, including neurodevelopment, synaptic plasticity, mood regulation, learning and memory, and recovery from neurological injuries. Maintaining optimal BDNF levels is essential for overall brain function and mental well-being.

The CR1 recombinant monoclonal antibody generation involves the retrieval of CR1 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. Subsequently, the CR1 recombinant monoclonal antibody is isolated from the culture supernatant of the transfected cell lines and is purified through affinity chromatography. After rigorous verification, the antibody can be used in ELISA and IHC applications, facilitating the precise detection of human CR1 protein.

Complement Receptor type 1 (CR1) is a multifunctional receptor that plays a central role in regulating the complement system. Its functions include complement cascade regulation, opsonization, immune complex clearance, immune tolerance, and the protection of host cells from complement-mediated damage. It is a critical component of both the innate and adaptive immune responses.

The CD59 recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, CD59 antibody genes are extracted from B cells isolated from immunoreactive rabbits. These genes are amplified and then cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies. The resulting CD59 recombinant monoclonal antibody is isolated from the culture supernatant of the transfected cell lines and undergoes affinity chromatography purification. After rigorous verification, the antibody can be used in ELISA and FC applications, allowing for precise detection of human CD59 protein.

CD59 is a crucial protein in the regulation of the complement system, preventing the formation of membrane attack complexes and protecting host cells from damage. Its role is essential in maintaining the integrity and function of various cells, particularly those in the blood and vascular system.

The synthesis of the C5AR1 recombinant monoclonal antibody involves a meticulous process to ensure its exceptional quality and specificity. It begins by isolating B cells from an immunized animal using the recombinant human C5AR1 protein as the immunogen. Total RNA is extracted from these B cells and converted into cDNA through reverse transcription. The C5AR1 antibody genes are then amplified using specific primers targeting the antibody constant regions and inserted into an expression vector. Through transfection, the vector is introduced into host cells, allowing for the production of the C5AR1 recombinant monoclonal antibody. Following cell culture, the antibody is harvested from the supernatant and subjected to purification using affinity chromatography, resulting in a highly purified form suitable for various applications. CUSABIO conducts ELISA to validate the antibody's specificity and functionality in detecting human C5AR1 protein.