The CD36 recombinant monoclonal antibody is synthesized in vitro through a multi-step process. Initially, CD36 antibody genes are isolated from B cells derived from immunoreactive rabbits. These genes are then subjected to amplification and cloning into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the generation of functional antibodies in substantial quantities. The resulting CD36 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography and is well-suited for ELISA and IHC applications, enabling the specific detection of human CD36 protein.

CD36 is a multifunctional cell surface receptor that plays a central role in the recognition, uptake, and metabolism of lipids and fatty acids. Its functions extend to immune responses, inflammation, and taste perception, making it a crucial protein involved in various physiological and pathological processes.

The EGR2 recombinant monoclonal antibody is synthetically generated in vitro, starting with the retrieval of EGR2 antibody genes from B cells obtained from immunoreactive rabbits. These EGR2 antibody genes are then amplified and cloned into appropriate phage vectors, which are subsequently introduced into mammalian cell lines to enable the production of functional antibodies in substantial quantities. Following this, the EGR2 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It is suitable for a range of applications, including ELISA, WB, and FC, facilitating the accurate detection of human and mouse EGR2 proteins.

EGR2 is a transcription factor that plays a central role in the development, myelination, and maintenance of the peripheral nervous system. Its functions are crucial for proper nerve function, and mutations in the EGR2 gene can lead to neurological disorders such as Charcot-Marie-Tooth disease. Additionally, EGR2 has been implicated in regulating cellular processes in cancer and nerve injury response.

The synthesis of the H2AFX recombinant monoclonal antibody entails a meticulously planned process involving recombinant DNA and in vitro cloning. The H2AFX antibody genes are cloned into expression vectors. Subsequently, these vectors are introduced into host cells, creating a conducive environment for the recombinant antibody's expression within a cell culture milieu. After expression, the antibody is subjected to affinity chromatography purification. Through rigorous testing, this antibody can be used in ELISA, IHC, and FC applications to detect human histone H2AX.

Histone H2AX and its phosphorylated form, γ-H2AX, are critical components of the cellular response to DNA damage. They serve as markers of DNA damage, enabling the recruitment of repair proteins to damaged sites and contributing to the maintenance of genomic integrity and cell viability.

The NPR2 recombinant monoclonal antibody is generated in vitro using synthetic genes. The technology involves recovering NPR2 antibody genes from B cells isolated from the immunoreactive rabbits, amplifying and cloning the genes into appropriate phage vectors, introducing the vectors into mammalian cell lines, and achieving expression of adequate amounts of functional antibody. The resulting NPR2 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It can be used in the ELISA, WB, IF, and FC applications to detect the human NPR2 protein.

NPR2 is a receptor for natriuretic peptides that plays a vital role in regulating blood pressure, fluid balance, and electrolyte homeostasis. Its activation promotes vasodilation, natriuresis, and diuresis, all of which help maintain cardiovascular and renal health while counteracting conditions like hypertension and heart failure.

The SOS1 recombinant monoclonal antibody production is a meticulously coordinated process involving recombinant DNA and in vitro cloning. The genes encoding both SOS1 antibody's heavy and light chains are seamlessly incorporated into expression vectors, which are transfected into host cells, facilitating the recombinant antibody's expression within a cell culture environment. Following expression, the antibody undergoes purification from the supernatant of transfected host cell lines through an affinity-chromatography purification method. This antibody shows reactivity with the human SOS1 protein. It can used in ELISA and FC applications.

SOS1 is a critical signaling protein that activates Ras, a central player in cell growth, proliferation, and differentiation. Its role in signal transduction pathways has broad implications for various physiological processes and diseases, making it an important target for research into cancer and other disorders.

The DDR2 recombinant monoclonal antibody synthesis is a meticulously orchestrated process. It all starts with in vitro cloning, where the genes encoding both DDR2 antibody's heavy and light chains are seamlessly incorporated into expression vectors. Following this, the expression vectors are introduced into host cells, enabling the recombinant antibody's expression within a cell culture environment. After expression, the antibody is carefully purified from the supernatant of transfected host cell lines, utilizing an affinity-chromatography purification method. This antibody can recognize both human and mouse DDR2 proteins in ELISA, WB, and FC applications.

DDR2 is a collagen receptor and receptor tyrosine kinase that plays a pivotal role in cell adhesion, migration, and tissue remodeling processes. Its functions are essential for normal development, tissue maintenance, and physiological responses to collagen-rich environments. Dysregulation of DDR2 signaling can have implications for various pathological conditions.

The INMT recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, INMT 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 INMT recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It can be used to detect human INMT protein in ELISA, IHC, and FC applications.

INMT is an enzyme responsible for the methylation of indolethylamines, producing methylated derivatives such as N-methyltryptamine and N-methylserotonin. While the exact biological functions of these methylated compounds are still being investigated, they are believed to play a role in neuromodulation and may have implications for neurotransmission and central nervous system function.

The production of the IL12B recombinant monoclonal antibody is a meticulously executed process involving in vitro cloning. The genes for both the heavy and light chains of the IL12B antibody are seamlessly integrated into expression vectors. Subsequently, these vectors are introduced into host cells, creating an environment conducive to the recombinant antibody's expression within a cell culture milieu. After expression, the antibody undergoes affinity chromatography purification. This antibody is recommended for the detection of the human IL12B protein in ELISA and FC applications.

IL12B protein, also known as the p40 subunit, when combined with the p35 subunit, forms the biologically active IL-12 cytokine, which plays a central role in immune responses, including the activation of immune cells, the differentiation of T cell subsets, and the regulation of immune functions critical for host defense against infections and cancer.

The PANX1 recombinant monoclonal antibody is a product of a carefully planned production process involving in vitro cloning. The genes responsible for both the heavy and light chains of the PANX1 antibody are seamlessly integrated into expression vectors. Subsequently, these vectors are introduced into host cells, paving the way for the recombinant antibody's expression within a cell culture setting. Post-expression, the antibody undergoes purification from the supernatant of transfected host cell lines through affinity chromatography. This antibody can be used to detect human PANX1 protein in a broad range of applications, including ELISA, IHC, IF, and FC.

The main function of the PANX1 protein is to serve as a channel in the cell membrane that allows the passage of ions and small molecules between the intracellular and extracellular environments. PANX1 channels are involved in various physiological and pathological processes, including cellular communication, inflammation, apoptosis, wound healing, and ion homeostasis.

The THEMIS recombinant monoclonal antibody production is a meticulously coordinated process. It commences with in vitro cloning, where genes encoding both THEMIS antibody's heavy and light chains are seamlessly incorporated into expression vectors, which are subsequently introduced into host cells, facilitating the recombinant antibody's expression within a cell culture environment. Following expression, the antibody undergoes purification from the supernatant of transfected host cell lines through an affinity-chromatography purification method. This antibody can detect the human THEMIS protein in four applications, including ELISA, IHC, IF, and FC.

THEMIS is a critical protein in the thymus that plays a central role in the development, selection, and function of T cells in the immune system. Its functions are crucial for the proper functioning of the adaptive immune response and the maintenance of immune tolerance.