Recombinant Rat Thrombopoietin Protein, CF 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 0.05-0.3 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived rat Thrombopoietin/Tpo protein Ser22-Ser326 |
Accession # |
|
N-terminal Sequence |
Starts at Ser22 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Thpo |
Purity |
>95%, 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 |
32.2 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 |
50-66 kDa, reducing conditions |
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 HCl. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat Thrombopoietin Protein, CF
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). Mature rat Tpo shares 68% and 81% aa sequence homology with human and mouse Tpo, respectively (4). 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. Tpo promotes the differentiation, proliferation, and maturation of megakaryocytes (MK) and their progenitors (5‑7). Several other cytokines can also promote these functions 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). These actions, in combination with direct effects on cardiomyocytes, can aid in the recovery of heart function following myocardial infarction (14). Tpo is cleaved by platelet‑derived thrombin following Arg191 within the C‑terminal domain and subsequently at other sites upon extended digestion (15). The C‑terminal domain is not required for binding to Tpo R or inducing MK growth and differentiation (6). 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 (16, 17).
- de Graaf, C.A. and D. Metcalf (2011) Cell Cycle 10:1582.
- Kaushansky, K. (2005) J. Clin. Invest. 115:3339.
- Li, J. et al. (1999) Br. J. Haematol. 106:345.
- Ogami, K. et al. (1995) Gene 158:309.
- Bartley, T.D. et al. (1994) Cell 77:1117.
- de Sauvage, F.J. et al. (1994) Nature 369:533.
- Kaushansky, K. et al. (1994) Nature 369:568.
- Kaushansky, K. et al. (1995) Proc. Natl. Acad. Sci. USA 92:3234.
- Broudy, V.C. et al. (1995) Blood 85:1719.
- Lok, S.I. et al. (1994) Nature 369:565.
- Chen, J. et al. (1995) Blood 86:4054.
- Oda, A. et al. (1996) Blood 87:4664.
- Van Os, E. et al. (2003) Br. J. Haematol. 121:482.
- Lupia, E. et al. (2012) Mediators Inflamm. 2012:390892.
- Kato, T. et al. (1997) Proc. Natl. Acad. Sci. 94:4669.
- Ehrenreich, H. et al. (2005) Proc. Natl. Acad. Sci. USA 102:862.
- Samoylenko, A. et al. (2008) Cell. Signal. 20:154.
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