Monoclonal Antibodies

This MERTK monoclonal antibody was generated through a process involving immunization of mice with recombinant MERTK protein (amino acids 21-505). Spleen cells from these immunized mice were then fused with myeloma cells, resulting in hybridomas. These hybridomas were subsequently screened to identify those producing the MERTK antibody, which were then cultured to obtain the final MERTK monoclonal antibody. This antibody exhibits high specificity for the human species. The MERTK monoclonal antibody is versatile and suitable for various applications including ELISA, Western Blotting, Immunohistochemistry, Immunofluorescence, and Flow Cytometry. It has been purified using protein A affinity chromatography, achieving a purity exceeding 95%.

MERTK plays a crucial role in regulating cellular processes, particularly phagocytosis, apoptosis, and inflammation. Its primary function is to facilitate the clearance of apoptotic cells and debris through a process known as efferocytosis. This is achieved by recognizing and binding to phosphatidylserine on the surface of apoptotic cells, initiating the phagocytosis process. Additionally, MERTK contributes to the regulation of inflammation by modulating the production of cytokines and chemokines.

The SMURF1 monoclonal antibody is produced through a meticulous process involving immunizing mice with recombinant human SMURF1 protein (amino acids 198-374). Subsequently, the immunized mouse B cells are fused with myeloma cells to generate hybridoma cells. After rigorous screening and selection, the SMURF1 antibody-secreting hybridomas are cultured in the mouse abdominal cavity. The SMURF1 monoclonal antibody is purified from the mouse ascites using protein G affinity chromatography, ensuring a purity exceeding 95%. This unconjugated IgG2a antibody exhibits high specificity for human SMURF1 protein, making it suitable for various applications including ELISA, Western blotting, immunohistochemistry, immunofluorescence, and flow cytometry.

SMURF1 is a protein-coding gene responsible for the production of an E3 ubiquitin ligase enzyme, which plays a crucial role in protein degradation. Its primary function lies in regulating the TGF-β signaling pathway by mediating the ubiquitination and subsequent degradation of specific proteins, including receptor-regulated SMADs (R-SMADs) and TGF-β receptors. SMURF1 exerts significant influence on various biological processes, including cell proliferation, differentiation, and apoptosis. Notably, dysregulation of this protein has been linked to a range of human diseases, such as cancer and skeletal dysplasia.

The Alix monoclonal antibody is produced through a meticulous process. Mice are immunized with recombinant human PDCD6IP protein, stimulating the production of antibodies. B cells from the immunized mice's spleen are then fused with myeloma cells, generating hybridoma cells. These cells are screened to identify the specific cell line that produces the Alix antibody. The antibody is then purified from the mouse ascites using protein A affinity chromatography, resulting in a purity exceeding 95%. This unconjugated IgG2b antibody is suitable for use in ELISA and WB applications, enabling the specific recognition of the human Alix protein.

Alix, also known as PDCD6IP, plays a critical role in various cellular processes, including endosomal sorting and multivesicular body (MVB) biogenesis. It interacts with the ESCRT machinery, mediating the sorting of ubiquitinated proteins into MVBs for degradation. Alix is also involved in cytokinesis, virus budding, and apoptosis. Its influence extends to the regulation of intracellular calcium signaling and has been implicated in various diseases, including cancer, HIV infection, and neurodegenerative disorders.