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In the production of the phospho-RB1 (S780) recombinant monoclonal antibody, the process commences with the extraction of RB1 antibody genes from immunized rabbits, originally exposed to a synthetic peptide derived from the human RB1 protein phosphorylated at S780. These isolated genes are then ingeniously inserted into expression vectors. Following this step, the modified vectors are skillfully introduced into host suspension cells, where they are diligently cultivated to stimulate the production and secretion of the antibodies. Subsequently, the phospho-RB1 (S780) recombinant monoclonal antibody is subjected to a rigorous purification technique involving affinity chromatography, enabling the separation of the antibody from the surrounding cell culture supernatant. Ultimately, the antibody's functionality is comprehensively assessed across a spectrum of assays, encompassing ELISA, IHC, IF, and IP tests, thereby confirming its capability to interact with human RB1 protein phosphorylated at S780.
Phosphorylation of retinoblastoma 1 (RB1) at S780 is often associated with the transition from the G1 phase to the S phase of the cell cycle, where cells prepare for DNA replication. When phosphorylated at S780, RB1 becomes inactivated, leading to the release of E2F transcription factors and allowing them to promote the transcription of genes required for cell cycle progression and cell proliferation. Dysregulation of RB1 phosphorylation at S780 can contribute to uncontrolled cell proliferation and is frequently observed in various cancers.
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