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The production of the HSPB1 recombinant monoclonal antibody employs DNA recombinant technology and in vitro genetic manipulation. Initially, an animal is immunized with a synthesized peptide derived from human HSPB1, and positive B cells are isolated and selected. The selected B cells undergo screening and single clone identification. The genes encoding the light and heavy chains of the HSPB1 antibody are then amplified through PCR and inserted into a plasmid vector to create a recombinant vector, which is introduced into a host cell line for antibody expression. The HSPB1 recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It exhibits specific reactivity towards human HSPB1 protein and is recommended for multiple applications, including ELISA, WB, IHC, IF, FC, and IP.
The HSPB1, also known as HSP27, acts as a molecular chaperone, helping to prevent protein aggregation and maintaining the proper conformation of proteins in the cell. It is involved in various cellular processes such as stress response, apoptosis, and protein quality control. HSPB1 plays a key role in protecting cells from various stressors, such as heat, oxidative stress, radiation, and toxic chemicals. HSPB1 has been shown to regulate apoptosis by inhibiting the activity of caspases.
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