TPO Human, CHO
Chinese Hamster Ovary Cells.
Greater than 98% as determined by SDS-PAGE.
Description
Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation.
The TPO is purified by proprietary chromatographic techniques.
Product Specs
| Thrombopoietin, a glycoprotein hormone primarily synthesized in the liver and kidneys, plays a crucial role in platelet production within the bone marrow. It acts by stimulating the production and differentiation of megakaryocytes, specialized bone marrow cells that fragment to release platelets. |
Recombinant Human Thrombopoietin, produced in CHO cells, exhibits a molecular weight range of 80-90kDa due to glycosylation. The purification process involves proprietary chromatographic techniques.
The TPO protein solution is formulated with phosphate buffered saline (pH 7.4) and 2% albumin.
While Thrombopoietin remains stable at room temperature for up to one week, it is recommended to store it between 2-8°C for optimal preservation.
The purity is determined to be greater than 98% using SDS-PAGE analysis.
The ED50, determined by dose-dependent stimulation of MO7e cells, corresponds to a specific activity of 3 x 105 units/mg.
Chinese Hamster Ovary Cells.
Product Science Overview
Thrombopoietin (TPO) is a crucial glycoprotein hormone primarily responsible for the regulation of platelet production in the body. It plays a significant role in the development and maturation of megakaryocytes, the bone marrow cells that produce platelets. Recombinant human thrombopoietin (rhTPO) produced in Chinese Hamster Ovary (CHO) cells is a biotechnologically engineered form of this hormone, designed to mimic the natural TPO in humans.
The concept of thrombopoietin was first introduced in 1958, but it wasn’t until 1994 that TPO was successfully purified and cloned by multiple research groups . This breakthrough allowed for the development of recombinant forms of TPO, including rhTPO and pegylated recombinant human megakaryocyte growth and development factor (PEG-rHuMGDF) .
TPO is primarily produced in the liver, but it is also synthesized in the kidney, bone marrow stroma, and other tissues . It binds to the TPO receptor (c-Mpl) on the surface of megakaryocytes and their progenitors, activating the JAK-STAT signaling pathway. This activation stimulates the growth and maturation of megakaryocytes, leading to increased platelet production .
Recombinant human TPO is produced in genetically modified CHO cells. These cells are widely used in biotechnology for the production of therapeutic proteins due to their ability to perform complex post-translational modifications, which are essential for the biological activity of many proteins . The rhTPO produced in CHO cells is supplied in a lyophilized form for clinical and research use .
The primary clinical application of rhTPO is in the treatment of thrombocytopenia, a condition characterized by low platelet counts. Thrombocytopenia can result from various causes, including chemotherapy, bone marrow disorders, and chronic liver disease . Clinical studies have shown that rhTPO is effective in increasing platelet counts in patients with chemotherapy-induced thrombocytopenia, immune thrombocytopenia, and myelodysplastic syndromes .
Despite its potential, the clinical use of rhTPO has faced challenges. Early recombinant TPO molecules led to the formation of neutralizing antibodies in some patients, which limited their effectiveness . However, second-generation TPO receptor agonists, such as romiplostim and eltrombopag, have been developed to overcome these issues . Ongoing research aims to further understand the biology of TPO and improve its therapeutic applications.
