Monoclonal Antibodies

The KRT19 monoclonal antibody is generated through a meticulous process involving immunization of mice with a synthetic peptide derived from human KRT19. B cells are subsequently isolated from the spleens of these immunized mice and fused with myeloma cells to create hybridomas. These hybridomas are rigorously screened to identify cell lines that secrete KRT19 antibodies. The selected hybridomas are then inoculated into the mouse abdominal cavity, and the KRT19 monoclonal antibodies are purified from the resulting mouse ascites through affinity chromatography using a specific immunogen.

This monoclonal antibody exhibits high specificity for human KRT19 protein, making it a valuable tool for both ELISA and IHC applications. It enables the precise detection and localization of KRT19 in tissues and cells.

KRT19, a type I intermediate filament protein, is prominently expressed in various epithelial cells, including those found in the liver, pancreas, colon, and breast. Its expression extends to certain non-epithelial cells, such as mesothelial and endothelial cells. KRT19 plays a pivotal role in maintaining the structural integrity of epithelial cells and is deeply involved in essential cellular processes such as signaling pathways, cell migration, and apoptosis. Furthermore, it has been implicated in the pathogenesis of several diseases, including cancer and liver disease.

This monoclonal antibody, specifically targeting human KRT5 protein, was developed using hybridoma technology. Mice were initially immunized with a synthetic peptide derived from human KRT5. Subsequently, B cells were isolated from their spleens and fused with myeloma cells to form hybridomas. From these hybridomas, those continuously producing the KRT5 antibody were screened and selected. The KRT5 antibody-secreting hybridomas were then cultured in the mouse abdominal cavity. The purified KRT5 monoclonal antibody was obtained from mouse ascites using a specific immunogen. This KRT5 monoclonal antibody has been validated in ELISA and IHC applications.

KRT5 is a type II intermediate filament protein primarily expressed in the basal cells of stratified epithelia. These include the epidermis of the skin, hair follicles, and nails. KRT5 functions to provide structural support and integrity to these tissues by forming a cytoskeletal network of filaments. Additionally, it plays a role in cell signaling pathways and gene regulation. Mutations in the KRT5 gene have been associated with several skin disorders, including epidermolysis bullosa simplex and Dowling-Degos disease.

This monoclonal antibody, specifically targeting human KRT8, was developed through hybridoma technology. The process involved immunizing mice with a synthetic peptide derived from human KRT8, followed by isolation of B cells from the immunized mice's spleens. These B cells were then fused with myeloma cells to generate hybridomas. From these hybridomas, those continuously producing the KRT8 antibody were carefully selected. The chosen hybridoma was then cultured in the mouse abdominal cavity. The KRT8 monoclonal antibody was subsequently purified from mouse ascites using specific immunogen affinity chromatography. This antibody has been validated for use in ELISA and IHC applications.

KRT8 is expressed in epithelial cells, particularly in simple epithelia lining the cavities of the body, such as the digestive and respiratory tracts. KRT8 plays a crucial role in providing structural support, maintaining the integrity of the cytoskeleton, protecting cells from mechanical stress and apoptosis, and participating in signal transduction, cell migration, and tumor progression.

The monoclonal antibody against human EPCAM was developed using hybridoma technology. The immunogen used for immunizing the mice was a synthetic peptide derived from human EPCAM. B cells were then isolated from the spleen of the immunized mouse and fused with myeloma cells to create hybridomas. The hybridomas were screened to identify those that produced the EPCAM antibodies and then cultured in the mouse abdominal cavity. The resulting monoclonal antibody was purified from mouse ascites using affinity chromatography with a specific immunogen. This EPCAM monoclonal antibody specifically reacts with human KRT14 protein and has been validated for use in ELISA and IHC applications.

EPCAM is a transmembrane glycoprotein that is expressed in various epithelial tissues. Its primary function is to mediate cell adhesion and signaling events between adjacent epithelial cells. EPCAM also plays a crucial role in cell proliferation, differentiation, migration, and apoptosis. Additionally, EPCAM is frequently employed as a diagnostic marker for epithelial tumors such as breast, colon, and ovarian cancers.

This ESR1 monoclonal antibody was produced using hybridoma technology. B cells were isolated from the spleen of a mouse immunized with a synthesized peptide derived from human ESR1. These B cells were then fused with myeloma cells to generate hybridomas. The hybridomas were screened to identify the clone producing continuous ESR1-specific antibodies, which was then cultured in the mouse abdominal cavity. The ESR1 monoclonal antibody was purified from mouse ascites using affinity chromatography with a specific immunogen, ensuring high purity. This purified ESR1 monoclonal antibody has been validated for its effectiveness in ELISA and IHC applications.

ESR1 plays a crucial role in regulating the female reproductive system, bone metabolism, and cardiovascular system. ESR1 binds to estrogen, forming a complex that regulates the expression of target genes involved in cell proliferation, differentiation, and apoptosis. Dysregulation of ESR1 has been linked to various diseases, including breast cancer and osteoporosis.