The PVR recombinant monoclonal antibody undergoes a comprehensive production process, commencing with in vitro cloning, where genes encoding the PVR antibody's heavy and light chains are incorporated into expression vectors. Subsequently, these vectors are transfected into host cells to enable recombinant antibody expression within a cell culture system. Post-expression, the PVR recombinant monoclonal antibody is purified from the supernatant of transfected host cell lines, employing an affinity-chromatography purification technique. An important feature of this antibody is its specific binding capability with the human PVR protein. Furthermore, its versatility shines through as it is suitable for diverse applications, encompassing ELISA, WB, and IHC.

The poliovirus receptor (PVR), also known as the CD155 receptor, mainly serves as a cell surface receptor for poliovirus and related enteroviruses. It plays a critical role in the initial attachment and entry of the virus into host cells.

The SOCS7 recombinant monoclonal antibody is generated via in vitro cloning, involving the integration of genes encoding both SOCS7 antibody's heavy and light chains into expression vectors. These vectors are then introduced into host cells to facilitate the recombinant antibody's expression within a cell culture context. Following expression, the SOCS7 recombinant monoclonal antibody is purified from the supernatant of transfected host cell lines, utilizing an affinity-chromatography-based purification method. Notably, this antibody exhibits high specificity in binding to the human SOCS7 protein and is remarkably versatile and suitable for three applications, including ELISA, IHC, and FC.

SOCS7 is a negative regulator of cytokine and growth factor signaling pathways, primarily through its involvement in the JAK-STAT pathway. Its function is to prevent excessive immune responses, regulate cell growth and differentiation, and maintain homeostasis. Dysregulation of SOCS7 can have implications for various diseases and conditions.

The PRKAR2A recombinant monoclonal antibody is created using in vitro expression systems, which are established by cloning the DNA sequences of PRKAR2A antibodies obtained from immunoreactive rabbits. The immunogen used in this process is a synthesized peptide derived from the human PRKAR2A protein. Subsequently, the genes encoding the PRKAR2A antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The PRKAR2A recombinant monoclonal antibody then undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA, IHC, IF, and FC applications, confirming its reactivity with the human PRKAR2A protein.

PRKAR2A is a regulatory subunit of PKA, a key enzyme involved in the cAMP signaling pathway. Through its role in regulating PKA activity, PRKAR2A influences a wide range of cellular processes, including metabolism, cell signaling, gene expression, and neurotransmitter release.

In vitro expression systems are used to generate the MICA recombinant monoclonal antibody, involving the cloning of MICA antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human MICA protein. Subsequently, the genes encoding the MICA antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. Post-expression, the MICA recombinant monoclonal antibody undergoes affinity-chromatography purification and is extensively tested for functionality in ELISA and IHC applications, confirming its reactivity with the human MICA protein.

MICA is a cell surface protein that serves as a critical ligand for the NKG2D receptor on immune cells, particularly NK cells and cytotoxic T cells. Its main role is to facilitate the recognition and elimination of cells under stress, infection, or transformation, contributing to immune surveillance, anti-cancer immunity, and the immune response against various pathogens.

The production of the DDB2 recombinant monoclonal antibody relies on in vitro expression systems, which are established by cloning the DNA sequences of DDB2 antibodies from immunoreactive rabbits. The immunogen used in this process is a synthesized peptide derived from the human DDB2 protein. Subsequently, the genes encoding the DDB2 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The DDB2 recombinant monoclonal antibody then undergoes purification through affinity chromatography and is subjected to extensive testing in ELISA, WB, IHC, and FC applications. These tests affirm its reactivity with the human DDB2 protein.

DDB2 is a DNA damage recognition protein that plays a central role in the NER pathway, which is responsible for identifying and repairing various types of DNA lesions, particularly those induced by UV radiation. Its function in DNA repair helps maintain genomic integrity and prevent mutations that can lead to cancer and other diseases.

In the production of the EBI3 recombinant monoclonal antibody, in vitro expression systems are utilized, entailing the cloning of EBI3 antibody DNA sequences from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human EBI3 protein. Subsequently, the genes encoding the EBI3 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. The EBI3 recombinant monoclonal antibody then undergoes purification through affinity chromatography and is subjected to extensive testing in ELISA and WB applications. These tests affirm its reactivity with the human EBI3 protein.

EBI3 is a crucial subunit of the IL-27 and IL-35 cytokines, which have diverse roles in the immune system. These cytokines can have both pro-inflammatory and anti-inflammatory functions, depending on the context, and are involved in immune regulation, infection control, and the maintenance of immune tolerance.

Through the utilization of in vitro expression systems, the NAIP recombinant monoclonal antibody is synthesized by cloning DNA sequences of NAIP antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human NAIP protein. Subsequently, the genes encoding the NAIP antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. The NAIP recombinant monoclonal antibody undergoes affinity-chromatography purification and is thoroughly tested for functionality in ELISA and IHC applications, displaying reactivity with the human NAIP protein during these evaluations.

NAIP is an important protein involved in the detection of intracellular bacterial pathogens and the initiation of an immune response through the activation of the NLRC4 inflammasome. Its role is essential in the host's defense against infections caused by bacteria that use type III secretion systems to manipulate host cells.

To produce the PKN2 recombinant monoclonal antibody, in vitro expression systems are harnessed, involving the cloning of DNA sequences of PKN2 antibodies obtained from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human PKN2 protein. Subsequently, the genes encoding the PKN2 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to enable antibody expression. The PKN2 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is extensively tested for functionality in ELISA, WB, and FC applications, confirming its reactivity with the human PKN2 protein.

PKN2 is a multifunctional protein kinase involved in a wide range of cellular processes, including cytoskeletal organization, cell migration, cell proliferation, and signaling pathways. Its diverse roles make it a crucial player in normal cellular physiology and contribute to its relevance in cancer biology and other diseases.

The AKT1/2/3 recombinant monoclonal antibody is created using in vitro expression systems, which are established by cloning the DNA sequences of AKT1/2/3 antibodies obtained from immunoreactive rabbits. The immunogen used in this process is a synthesized peptide derived from the human AKT1/2/3 protein. Subsequently, the genes encoding the AKT1/2/3 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate antibody expression. The AKT1/2/3 recombinant monoclonal antibody then undergoes affinity-chromatography purification and is rigorously tested for functionality in ELISA, WB, IHC, and FC applications, confirming its reactivity with the human AKT1/2/3 protein.

AKT1, AKT2, and AKT3 are closely related isoforms of the AKT protein kinase family. While they share structural similarities and some functional overlap, they exhibit distinct tissue-specific expression patterns and play specialized roles in various cellular processes. AKT1 is widely expressed in various tissues and is involved in the regulation of cell growth, survival, and proliferation. AKT2 is predominantly expressed in insulin-responsive tissues such as skeletal muscle, liver, and adipose tissue, and plays a crucial role in glucose homeostasis and insulin signaling. AKT3 is expressed at higher levels in the brain and nervous system, where it contributes to neuronal development and function.

Through the utilization of in vitro expression systems, the HSD3B1 recombinant monoclonal antibody is synthesized by cloning DNA sequences of HSD3B1 antibodies sourced from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human HSD3B1 protein. Subsequently, the genes encoding the HSD3B1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. The HSD3B1 recombinant monoclonal antibody undergoes affinity-chromatography purification and is rigorously tested for functionality in ELISA, IHC, IF, and FC applications, displaying reactivity with the human HSD3B1 protein during these assessments.

HSD3B1 is a key enzyme in steroidogenesis, catalyzing the conversion of pregnenolone to progesterone. Its activity is essential for the production of various steroid hormones, including sex steroids, glucocorticoids, and mineralocorticoids, which have critical roles in reproductive function, stress response, and various physiological processes in both males and females.