The LGR6 recombinant monoclonal antibody is synthetically generated in vitro, employing a multi-step process. Initially, LGR6 antibody genes are isolated from B cells sourced from immunoreactive rabbits. These LGR6 antibody genes are then amplified and cloned into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies in significant quantities. The resulting LGR6 recombinant monoclonal antibody is purified from the culture supernatant of these transfected cell lines through affinity chromatography. It is well-suited for various applications, including ELISA, IHC, IF, and FC, enabling the precise detection of human LGR6 protein.

LGR6 is a cell-surface receptor protein involved in the regulation of tissue development, regeneration, and stem cell maintenance in various tissues, including the skin, hair follicles, and mammary glands. Its role in maintaining stem cell populations and regulating tissue homeostasis is crucial for normal tissue function and repair.

The BRIP1 recombinant monoclonal antibody is created using synthetic genes through in vitro methods. This process entails the retrieval of BRIP1 antibody genes from B cells obtained from immunoreactive rabbits, followed by gene amplification and insertion into suitable phage vectors. These vectors are then introduced into mammalian cell lines, enabling the production of functional antibodies in substantial quantities. Subsequently, the BRIP1 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography and is suitable for ELISA and WB applications, facilitating the detection of human BRIP1 protein.

BRIP1 is a DNA helicase protein that plays a crucial role in DNA repair processes, particularly in the context of homologous recombination and genome stability maintenance. Its interaction with BRCA1 and involvement in the Fanconi anemia pathway are essential for the repair of DNA damage and the prevention of cancer development. Mutations in BRIP1 can increase the risk of hereditary breast and ovarian cancer.

The synthesis of the FTL recombinant monoclonal antibody entails a meticulously planned process involving in vitro cloning. First, the FTL antibody genes are seamlessly incorporated into expression vectors, which are then introduced into host cells, creating a conducive environment for the recombinant antibody's expression within a cell culture milieu. After expression, the antibody is purified from the supernatant of the transfected host cells through affinity chromatography. This antibody displays a specific binding affinity for the human FTL protein in ELISA, IHC, and FC applications.

The ferritin light chain (FTL) is a crucial component of the ferritin protein complex, which is responsible for the storage, regulation, and release of iron within cells. This function is vital for maintaining iron homeostasis, protecting against oxidative stress, and supporting various cellular metabolic processes.

The LAMP2 recombinant monoclonal antibody production is a meticulously orchestrated process. It initiates with in vitro cloning, where genes for both the heavy and light chains of the LAMP2 antibody are seamlessly incorporated into expression vectors. Subsequently, these modified vectors are introduced into host cells, creating a conducive environment for the recombinant antibody's expression within a cell culture milieu. After expression, the LAMP2 recombinant monoclonal antibody is subjected to a rigorous purification process, making use of affinity chromatography. A notable characteristic of this antibody is its specific binding affinity for the human LAMP2 protein. It is recommended for use in ELISA and IHC.

LAMP2 plays a central role in the proper functioning of lysosomes, which are essential for cellular waste disposal, recycling of cellular components, and various other cellular processes. Dysfunction or deficiency of LAMP2 can lead to lysosomal storage diseases and other health conditions.

The DDIT3 recombinant monoclonal antibody production is a meticulously planned journey. It begins with in vitro cloning, where genes encoding both DDIT3 antibody's heavy and light chains are seamlessly incorporated into expression vectors, which are introduced into host cells, facilitating the recombinant antibody's expression within a cell culture environment. Following expression, the DDIT3 recombinant monoclonal antibody is subjected to affinity-chromatography purification. A noteworthy feature of this antibody is its specific binding to the human DDIT3 protein. It is suitable for ELISA and FC applications.

DDIT3 is a multifunctional transcription factor that plays a crucial role in the cellular response to stress signals, including ER stress and DNA damage. Its functions include regulating gene expression, determining cell fate under stress conditions, and influencing various cellular processes, such as metabolism and inflammation, to help cells adapt to or cope with stress.

The recombinant RIOX2 antibody is a monoclonal antibody made in vitro using the RIOX2 antibody genes that are typically expressed from a plasmid in a stable mammalian cell line. The genes coding for the RIOX2 antibody will ultimately assemble into a fully functional antibody after translation. The synthesized antibody is the recombinant antibody against RIOX2. It underwent purification using affinity-chromatography. This recombinant RIOX2 antibody is suitable for use in the ELISA to detect the RIOX2 protein from Human.

RIOX2, a JmjC (Jumonji-C) domain-containing 2-oxoglutarate (2OG)-dependent oxygenase, is implicated in gene transcription in eukaryotic cells. It promotes cell proliferation, cycle transition, and anti-apoptosis carcinogenic activities. RIOX2 upregulation has been found in several human solid and hematological malignancies, including colon, esophagus, lung, lymphocyte, kidney, nervous system, liver, breast, pancreas, and gastric cancers. Enhanced RIOX2 expression has been associated with a poor prognosis, and evidence has shown that RIOX2 downregulation inhibits cancer cell growth and survival.

The POSTN recombinant monoclonal antibody synthesis is a meticulously orchestrated process. It all starts with in vitro cloning, where the POSTN antibody genes 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 is only reactive with the human POSTN protein. It is suitable for three applications, including ELISA, IHC, and FC.

The main function of POSTN (Periostin) protein is to serve as an extracellular matrix (ECM) protein that plays a role in tissue development, repair, and remodeling. POSTN is secreted by various cell types and is involved in several physiological and pathological processes, including cardiac health, allergic responses, tumor microenvironment, tissue homeostasis, and dental health.

The production of the HLA-G recombinant monoclonal antibody is a meticulously executed process. It initiates with in vitro cloning, where HLA-G antibody genes are seamlessly integrated into expression vectors. Subsequently, these vectors are transfected into host cells, creating an environment conducive to the recombinant antibody's expression within a cell culture milieu. After that, the HLA-G recombinant monoclonal antibody is subjected to affinity chromatography purification. This antibody specifically binds to the human HLA-G protein in ELISA and FC.

HLA-G is a critical immunomodulatory molecule involved in immune tolerance, immune regulation, and immune evasion. Its functions are particularly significant during pregnancy, in cancer biology, and in various pathological conditions where immune responses need to be controlled or suppressed.

The HIST1H1C recombinant monoclonal antibody is a product of a carefully planned production process. It commences with in vitro cloning, where the HIST1H1C antibody genes 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 HIST1H1C recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines through affinity chromatography. This antibody shows a specific binding affinity for the human HIST1H1C protein in ELISA, IHC, IF, and FC applications.

HIST1H1C, also called Histone H1.2, like other histone proteins, plays a significant role in the packaging and organization of DNA within the cell nucleus. Specifically, its main function is related to chromatin compaction and gene regulation.

The synthesis of the CRP recombinant monoclonal antibody entails a meticulously planned process. It commences with in vitro cloning, where the genes encoding both CRP antibody's heavy and light chains 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 environment. Following expression, the CRP recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines, a purification process that leverages affinity chromatography. An impressive attribute of this antibody is its specific binding affinity for the human CRP protein. Moreover, its versatility is a standout feature, as it is well-suited for ELISA and IHC applications.

The main role of C-reactive protein (CRP) is as a biomarker of inflammation and infection in the body. CRP is produced by the liver in response to inflammation, infection, or tissue injury. Its primary function is to bind to damaged cells, foreign invaders (such as bacteria), and other substances in the blood that are associated with inflammation. CRP acts as part of the body's innate immune system, helping to recognize and target potential threats.