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T4184
Sigma
Thrombopoietin from mouse
>97% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder, cell culture tested
| Synonym: | TPO |
| MDL number: | MFCD01095336 |
Description
| Analysis Note | The biological activity was measured in a cell proliferation assay using MO7e cells. |
| Physical form | Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing 0.25 mg bovine serum albumin |
| Biochem/physiol Actions | Thrombopoeitin (TPO), also known as the ligand for the c-mpl proto-oncogene (Mpl-L) and as megakaryocyte colony stimulating factor (Meg-CSF), is a primary regulatory factor for megakaryocytopoiesis and thrombopoiesis.1,2,3,4 Produced mainly by hepatocytes but also by kidney cells, TPO is a humoral glycoprotein that stimulates growth and maturation of megakaryocytes and megakaryocytic colonies from bone marrow cultures. TPO binds and activates an 68-78 kDa glycoprotein receptor belonging to the GH family of cytokine receptors, a family that includes receptors to growth hormone (GH), erythropoietin (EPO) and prolactin (PRL).5,6 Like GH and EPO, TPO may bind to its receptor at two distinct sites, initiating receptor dimerization and activation.7 Analysis of mRNA indicates also the existence of a novel truncated and potentially soluble form of TPO receptor. The viral oncogene v-mlp of the myeloproliferative leukemia virus (MPLV) contains the gene sequence for the entire cytoplasmic and transmembrane domains and a portion of the extracellular domain of c-mlp (TPO receptor). TPO receptors are found on megakaryocytes and their precursors and on platelets. The mature form of TPO is a highly conserved glycoprotein, showing approximately 70% sequence homology among various mammals. Human TPO contains 332 amino acids (mouse 335) including two internal disulfide bonds and 6 N-linked glycosylation sites (mouse 7). The N-terminal 153 amino acid region of TPO shows structural and amino acid sequence homology to erythropoietin and a pair of arginines (potential cleavage site) separating it from the highly glycosylated carboxyterminal domain. |
Properties
| recombinant | expressed in NSO cells |
| assay | >97% (SDS-PAGE) |
| form | lyophilized powder |
| mol wt | mol wt ~75 kDa by SDS-PAGE (as a result of glycosylation) |
| predicted mol wt 35 kDa | |
| total impurities | Endotoxin, tested |
| suitability | cell culture tested |
| Gene Information | mouse ... Thpo(21832) |
| storage temp. | −20°C |
Safety
| Personal Protective Equipment | Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter |
| WGK Germany | 3 |
References
| Cited Reference | 1. Lok, S., and Foster, D., The structure, biology and potential therapeutic applications of recombinant thrombopoietin. Stem Cells 12, 586-598, (1994) |
| 2. Kato, T., et al., Native thrombopoietin: structure and function. Stem Cells 16, 11-19, (1998) | |
| 3. , Kuter, D., et al., eds. Thrombopoiesis and Thrombopoietins Totowa, N.J , (1997) | |
| 4. Callard, R., and Gearing, A. The Cytokine Facts Book New York , (1994) | |
| 5. Heim, M.H., The Jak-STAT pathway: cytokine signalling from the receptor to the nucleus. Receptor Signal Transduction Res. 19, 75-120, (1999) | |
| 6. Skoda, R., Specificity of signaling by hematopoietic cytokine receptors: instructive versus permissive effects. J. Recept. Signal Transduct. Res. 19, 741-772, (1999) | |
| 7. Hou, J., Zhan, H., Expression of active thrombopoietin and identification of its key residues responsible for receptor binding. Cytokine 10, 319, (1998) | |
| reference | Avanzi, G., et al., Selective growth response to IL-3 of a human leukemic cell line with megakaryoblastic features. Br. J. Haematol. 69, 359-366, (1988) |




