Human Thrombopoietin R/Tpo R Biotinylated Antibody Summary
Gln26-Tyr423
Accession # P40238
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Thrombopoietin R/Tpo R
Thrombopoietin receptor (Tpo R), also known as myeloproliferative leukemia protein (c-mpl), is a 95 kDa type I transmembrane protein that is a member of the type I cytokine receptor family within the hematopoietin/cytokine receptor superfamily (1 - 4). The 635 amino acid (aa) full-length human Tpo R contains a 25 aa signal sequence, a 466 aa extracellular domain with a ligand binding domain and two fibronectin type III domains, a transmembrane (TM) domain and a cytoplasmic domain. The extracellular domain of human Tpo R shares 78%, 76%, 81%, 82% and 80% aa identity with mouse, rat, bovine, canine and equine Tpo R, respectively. Humans produce three distinct mRNA species; a P-form, a K-form, and a truncated form (Mpl-tr) lacking a TM domain (3 - 7). The P-form encodes the full-length receptor. The Mpl-tr form, which is expressed in both human and mouse, is intracellular and targets the P-form for degradation (5, 6). The 579 aa K-form has an alternate cytoplasmic domain, but does not dimerize with, or inhibit, the P-form (7). Thrombopoietin (Tpo) is a key regulator of megakaryocytopoiesis, thrombopoiesis and hematopoietic stem cell self-renewal, as reflected by expression of the Tpo R on megakaryocytes, platelets and hematopoietic progenitors (2, 8). Receptor dimerization occurs upon Tpo binding and initiates signaling through the Ras/MAP and JAK/STAT pathways (1, 2). Internalization and degradation of Tpo following Tpo R binding serves to downregulate circulating Tpo (9). Tpo R expressed at low levels on endothelial cells does not appear to contribute to regulation of Tpo (10). Inactivating mutations of Tpo R cause thrombocytopenia, and absence of functional Tpo R is lethal in humans, but not mice. Other mutations, including an activating change in the TM domain, can cause thrombocytosis (11, 12).
- Kaushansky, K. (2005) J. Clin. Invest. 115:3339.
- Deutsch, V.R. and A. Tomer (2006) Br. J. Haematol. 134:453.
- Vigon, I. et al. (1992) Proc. Natl. Acad. Sci. USA 89:5640.
- Mignotte, V. et al. (1994) Genomics 20:5.
- Li, J. et al. (2000) Cytokine 12:835.
- Coers, J. et al. (2004) J. Biol. Chem. 279:36397.
- Millot, G.A. et al. (2002) Exp. Hematol. 30:166.
- Tong, W. et al. (2007) Exp. Hematol. July 14 [Epub ahead of print].
- Li, J. et al. (1999) Br. J. Haematol. 106:345.
- Geddis, A.E. et al. (2006) Exp. Hematol. 34:82.
- Germeshausen, M. et al. (2006) Hum. Mutat. 27:296.
- Ding, J. et al. (2004) Blood 103:4198.
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