The preparation of the AQP4 recombinant monoclonal antibody entails a meticulously planned process. It all starts with in vitro cloning, where AQP4 antibody genes are seamlessly incorporated into expression vectors. Subsequently, these vectors are transfected into host cells, creating a conducive environment for the recombinant antibody's expression within a cell culture milieu. After expression, the AQP4 recombinant monoclonal antibody is subjected to affinity chromatography purification. This antibody is well-suited for ELISA and IHC to detect human AQP4 protein.

AQP4 is a crucial protein for maintaining water homeostasis and fluid balance in the CNS and other tissues. Dysregulation of AQP4 function can have implications for neurological disorders, brain injuries, and conditions affecting fluid balance in various organs.

The KRT10 recombinant monoclonal antibody production is a meticulously coordinated process. It commences with in vitro cloning, where KRT10 antibody genes are seamlessly incorporated into expression vectors. Subsequently, these vectors are introduced into host cells, facilitating the recombinant antibody's expression within a cell culture environment. Following expression, the KRT10 recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines through an affinity-chromatography purification method. This antibody only recognizes the human KRT10 protein. It has been tested for ELISA and IHC applications.

KRT10 plays a central role in maintaining the structural integrity of the epidermis, contributing to the formation of a protective skin barrier, and facilitating the process of epidermal differentiation and cornification. Its proper function is essential for healthy skin, and mutations in the KRT10 gene can lead to skin disorders characterized by skin fragility and abnormalities.

The RELB recombinant monoclonal antibody production is a meticulously orchestrated process. It commences with in vitro cloning, where genes for both the heavy and light chains of the RELB antibody are seamlessly incorporated into plasmid vectors. Following this, these recombinant vectors are introduced into host cells, creating a conducive environment for the recombinant antibody's expression within a cell culture context. Post-expression, the RELB recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines, relying on the effectiveness of affinity chromatography. A remarkable characteristic of this antibody is its high specificity in binding to the human RELB protein. Furthermore, its versatility is evident, making it suitable for a diverse range of applications, including ELISA, IF, and FC.

RELB is a member of the Rel/NF-κB family of transcription factors, which play critical roles in controlling various cellular processes, particularly those related to the immune system and inflammation. Its activity is tightly controlled to ensure an appropriate response to immune challenges while avoiding excessive inflammation and autoimmune reactions.

The MFN1 recombinant monoclonal antibody is a product of a comprehensive production process. This journey begins with in vitro cloning, where the genes responsible for both the heavy and light chains of the MFN1 antibody are seamlessly integrated into expression vectors. Subsequently, these vectors are introduced into host cells, facilitating the recombinant antibody's expression within a cell culture environment. After expression, the MFN1 recombinant monoclonal antibody is subjected to a rigorous purification process, drawing on the capabilities of affinity chromatography. A noteworthy characteristic of this antibody is its specific reactivity with the human MFN1 protein. Additionally, its versatility shines through as it is suitable for ELISA and FC applications.

MFN1 protein mainly facilitates mitochondrial fusion by tethering the outer membranes of adjacent mitochondria together, thus allowing them to fuse and exchange contents, including proteins and lipids. MFN1 is implicated in regulating mitochondrial dynamics, including the balance between fusion and fission, which is essential for cellular homeostasis and adaptation to various cellular stress conditions.

The production of the ALPP recombinant monoclonal antibody is a meticulously coordinated process. It initiates with in vitro cloning, where genes for both the heavy and light chains of the ALPP antibody are seamlessly integrated into expression vectors. Subsequently, these vectors are introduced into host cells, enabling the recombinant antibody's expression within a cell culture context. Following expression, the ALPP recombinant monoclonal antibody is carefully purified from the supernatant of transfected host cell lines, making use of the precision of affinity chromatography. A salient feature of this antibody is its specific binding to the human ALPP protein. Moreover, its versatility is evident, as it is well-suited for a wide array of applications, including ELISA and FC.

The main role of the ALPP protein is to catalyze the hydrolysis of phosphate esters in an alkaline environment. ALPP is commonly found in various tissues, including the placenta, liver, bone, and kidney. In the placenta, ALPP plays a crucial role in nutrient transport and metabolism during pregnancy. In bone tissue, it is involved in mineralization processes. In clinical settings, the measurement of ALPP levels is used as a diagnostic marker for various medical conditions, including liver disease and certain bone disorders.

The STAT1 recombinant monoclonal antibody is the result of a meticulously orchestrated production process. It commences with in vitro cloning, where genes encoding both the heavy and light chains of the STAT1 antibody are seamlessly incorporated into expression vectors. Subsequently, these vectors are introduced into host cells, paving the way for the recombinant antibody's expression within a cell culture milieu. After expression, the STAT1 recombinant monoclonal antibody is subjected to a precise purification process, reliant on the effectiveness of affinity chromatography. A remarkable characteristic of this antibody is its high specificity in binding to the human STAT1 protein. Furthermore, its adaptability is evident, as it is suitable for a diverse range of applications, including ELISA, IHC, IF, and FC.

STAT1 is a versatile transcription factor that plays a crucial role in immune responses, antiviral defense, inflammation, cell growth, and differentiation. Dysregulated STAT1 signaling can contribute to autoimmune diseases by promoting excessive immune responses and inflammation and is associated with increased cancer risk.

The MAP1LC3B recombinant monoclonal antibody is generated via a meticulously executed process. It initiates with in vitro cloning, where genes encoding both the heavy and light chains of the MAP1LC3B antibody are incorporated into expression vectors, which are subsequently introduced into host cells, setting the stage for the recombinant antibody's expression within a cell culture environment. Following expression, the MAP1LC3B recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines, relying on the precision of affinity chromatography. An outstanding attribute of this antibody is its specific binding affinity for the human MAP1LC3B protein. Additionally, it is known for its versatility, making it suitable for an array of applications, including ELISA, WB, and FC.

MAP1LC3B is a critical protein in the autophagy pathway, where it plays a central role in autophagosome formation, cargo recognition, and autophagosome-lysosome fusion. It is also involved in quality control mechanisms within cells. MAP1LC3B helps remove damaged organelles, misfolded proteins, and protein aggregates, contributing to the maintenance of cellular health and preventing the accumulation of potentially harmful materials.

The production of the DPYSL2 recombinant monoclonal antibody is a meticulously executed process. It initiates with in vitro cloning, where genes for both the heavy and light chains of the DPYSL2 antibody are cloned 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 setting. After expression, the DPYSL2 recombinant monoclonal antibody is purified from the cell culture supernatant through affinity chromatography. A remarkable feature of this antibody is its specific binding to the human DPYSL2 protein. Furthermore, its versatility is evident, as it is well-suited for various applications, including ELISA, IHC, IF, and FC.

DPYSL2 is a multifunctional protein that plays a central role in nervous system development and function. It is involved in neurite outgrowth, axon guidance, synaptic plasticity, neuronal signaling, and neuronal survival. Dysregulation of DPYSL2 has implications for various neurological disorders and conditions.

The LYVE1 recombinant monoclonal antibody synthesis is a meticulously orchestrated process. It all starts with in vitro cloning, where the genes encoding both LYVE1 antibody's heavy and light chains are cloned into plasmid vectors. After that, these vectors are transfected into host cells, enabling the recombinant antibody's expression within a cell culture environment. After expression, the LYVE1 recombinant monoclonal antibody is carefully purified from the supernatant of transfected host cell lines, utilizing an affinity-chromatography purification method. This antibody exclusively shows reactivity with the human LYVE1 protein. Additionally, its versatility shines through, as it is suitable for various applications, including ELISA, IF, and FC.

LYVE1 is a crucial protein for the normal functioning of the lymphatic system, particularly in the uptake and transport of hyaluronan and other molecules. Its role in lymphatic biology has implications for various physiological processes, including tissue fluid balance, immune responses, and pathological conditions such as cancer metastasis.

The IKZF1 recombinant monoclonal antibody is a product of a carefully planned production process. It commences with in vitro cloning, where the genes responsible for both the heavy and light chains of the IKZF1 antibody are seamlessly inserted into expression vectors. Subsequently, these vectors are transfected into host cells, paving the way for the recombinant antibody's expression within a cell culture milieu. Post-expression, the IKZF1 recombinant monoclonal antibody undergoes purification from the supernatant of transfected host cell lines through the precision of affinity chromatography. This antibody shows a specific binding affinity for the human IKZF1 protein. It is suitable for ELISA and FC applications.

IKZF1 is a key transcription factor that plays a central role in lymphocyte development, immune system function, and the regulation of genes involved in immune responses. Its proper functioning is essential for a well-balanced and effective immune system.