Thrombopoietin is a member of the EPO/TPO family and is composed of an N-terminal domain that shares structural similarities with erythropoietin (EPO). The mature mouse TPO protein has a molecular weight of approximately 80-85 kDa and consists of 356 amino acids . The protein sequence of mouse TPO shares significant homology with human and rat TPO, with 71% and 81% sequence identity, respectively .
The primary function of TPO is to regulate the production and maturation of megakaryocytes, the precursor cells that give rise to platelets. TPO achieves this by binding to its receptor on the surface of megakaryocytes and their progenitor cells, stimulating their proliferation and differentiation . This process is essential for maintaining normal platelet levels in the blood and ensuring proper blood clotting and wound healing.
Recombinant mouse thrombopoietin is produced using various expression systems, including insect cells and mouse myeloma cell lines . The recombinant protein is typically purified to high levels of purity (>95%) and is biologically active, meaning it can elicit a biological response in vitro and in vivo . It is often used in research to study the mechanisms of thrombopoiesis and to develop therapeutic strategies for platelet disorders.
Recombinant mouse thrombopoietin is widely used in scientific research for various applications, including: