Recombinant Mouse Thrombopoietin Protein Summary
Details of Functionality |
Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. Avanzi, G. et al. (1988) Br. J. Haematol. 69:359. The ED50 for this effect is 0.4-2.4 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse Thrombopoietin/Tpo protein Ser22-Thr356 |
Accession # |
|
N-terminal Sequence |
Ser22 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Thpo |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
35 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
80-90 kDa, reducing conditions |
Publications |
Read Publications using 488-TO in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Thrombopoietin Protein
Background
Thrombopoietin (Tpo), is a key regulator of megakaryocytopoiesis and thrombopoiesis. It is principally produced in the liver and is bound and internalized by the receptor Tpo R/c-mpl. Defects in the Tpo-Tpo R signaling pathway are associated with a variety of platelet disorders (1-3). The 356 amino acid (aa) mouse Tpo precursor is cleaved to yield the 335 aa mature protein. Mature mouse Tpo shares 71% and 81% aa sequence homology with human and rat Tpo, respectively. It is an 80-85 kDa protein that consists of an N-terminal domain with homology to Erythropoietin (Epo) and a C-terminal domain that contains multiple N-linked and O-linked glycosylation sites (4, 5). Tissue specific alternate splicing of mouse Tpo generates multiple isoforms with internal deletions, insertions, and/or C-terminal substitutions (6). Tpo promotes the differentiation, proliferation, and maturation of MK and their progenitors (4, 5, 7). Several other cytokines can promote these functions as well but only in cooperation with Tpo (8, 9). Notably, IL-3 independently induces MK development, although its effects are restricted to early in the MK lineage (8, 9). Tpo additionally promotes platelet production, aggregation, ECM adhesion, and activation (10-13). It is cleaved by platelet-derived thrombin following Arg191 within the C‑terminal domain and subsequently at other sites upon extended digestion (14). Full length Tpo and shorter forms circulate in the plasma (4, 5). The C‑terminal domain is not required for binding to Tpo R or inducing MK growth and differentiation (5). Aside from its hematopoietic effects, Tpo is expressed in the brain where it promotes the apoptosis of hypoxia-sensitized neurons and inhibits neuronal differentiation by blocking NGF-induced signaling (15, 16).
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Deutsch, V.R. and A. Tomer (2006) Br. J. Haematol. 134:453.
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Kaushansky, K. (2005) J. Clin. Invest. 115:3339.
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Li, J. et al. (1999) Br. J. Haematol. 106:345.
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Bartley, T.D. et al. (1994) Cell 77:1117.
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de Sauvage, F.J. et al. (1994) Nature 369:533.
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Marcucci, R. and M. Romano (2008) Biochim. Biophys. Acta 1782:427.
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Kaushansky, K. et al. (1994) Nature 369:568.
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Kaushansky, K. et al. (1995) Proc. Natl. Acad. Sci. 92:3234.
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Broudy, V.C. et al. (1995) Blood 85:1719.
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Lok, S.I. et al. (1994) Nature 369:565.
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Chen, J. et al. (1995) Blood 86:4054.
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Oda, A. et al. (1996) Blood 87:4664.
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Van Os, E. et al. (2003) Br. J. Haematol. 121:482.
-
Kato, T. et al. (1997) Proc. Natl. Acad. Sci. 94:4669.
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Ehrenreich, H. et al. (2005) Proc. Natl. Acad. Sci. 102:862.
- Samoylenko, A. et al. (2008) Cell. Signal. 20:154.
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