EPO Structure – Boster Bio

1. EPO Structure – Boster Bio EPO (Epo antibody) is a gene with five exons and four intros that is discovered on chromosome 7. This gene produces a 193-base amino acid chain as a transcriptional product. The chain is changed to 166 amino acids during translation. The hydrophobic amino acids make up the majority of the cleaved 27 amino acid leader sequence. The C-terminus loses its final arginine residue once the translation is completed, resulting in a final length of 165 amino acids residues. The peptide backbone weighs 18 kDa and the total glycoprotein measures 30 kDa. EPO is a glycoprotein made up entirely of Alpha Helixes. The cysteine residues’ sulfur binds together to form disulfide bonds. EPO’s structure is maintained by these disulfide bonds. The hematopoietic cytokine family includes the EPO (Epo antibody) receptor in the blood marrow. This receptor has a single transmembrane domain that forms a homodimer complex until EPO binds to it and activates it. This receptor has a length of 484 amino acids and a mass of 52.6 kDa. After the homodimer is formed as a result of the interaction, the Jak2 kinases undergo autophosphorylation, which stimulates other cellular processes. There are two extracellular domains in this transmembrane receptor. The cysteine residues Cys67 and Cys83, as well as Cys28 and Cys38, form two disulfide linkages in this receptor. This receptor’s intracellular region, unlike other receptors, has no enzymatic activity.