Recombinant Mouse Pleiotrophin/PTN Protein, CF Summary
Product Specifications
Met1-Asp168
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
6580-PL
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Pleiotrophin/PTN
Pleiotrophin (PTN), also called heparin-binding growth-associated molecule (HB-GAM), heparin-binding neurotrophic factor (HBNF), heparin-affinity regulatory peptide (HARP), or osteoblast-specific factor (OSF-1), is an 18 kDa secreted, strongly heparin-binding, developmentally regulated cytokine (1 ‑ 3). PTN and midkine share 50% amino acid (aa) sequence identity, share some functions, and constitute a family (1 ‑ 3). The mouse PTN cDNA encodes 168 aa, including a 32 aa signal sequence and two thrombospondin type 1 (TSP1) beta sheet domains separated by a linker and flanked by lysine-rich N- and C-terminal sequences (4). The second TSP1 domain (aa 97 ‑ 129) contains the highest affinity binding site for heparin (4, 5). A 15 kDa form which lacks the C-terminus is mitogenic for glioblastoma cells, while full-length PTN is not (6). PTN is a highly conserved protein; human, mouse, rat, canine, porcine, equine and bovine PTN share 98% aa sequence identity or greater. During development, PTN is involved in development of brain, bone, and organs undergoing branching morphogenesis (3). In the adult, it is induced by PDGF and upregulated in many cancers, hematopoietic stem cells and tissues undergoing remodeling (7 ‑ 10). Cell surface receptors for PTN include Syndecan-3 (which mediates neurite outgrowth) and the receptor tyrosine phosphatase PTPRB, also called RPTP beta / zeta (3, 11 ‑ 13). Heparin binding is necessary for engaging these receptors (7, 8). PTN causes PTPRB dimerization and inactivates its phosphatase activity, which allows increased tyrosine phosphorylation of its substrates (12 ‑ 14). One such substrate is the WNT pathway molecule beta -catenin, allowing crosstalk of PTN with WNTs (12). PTN activation of the receptor ALK (anaplastic lymphoma kinase) is indirect through PTPRB, and mediates mitogenic, transforming and angiogenic activities of PTN (2, 5, 6, 13). Increased expression of PTN is correlated with neuronal development or stresses such as brain ischemia and Parkinson’s disease (2, 3, 7, 8). Both PTN and midkine have demonstrated bactericidal activity, but only in the absence of heparin (15).
- Naito, A. et al. (1992) Biochem. Biophys. Res. Commun. 183:701.
- Perez-Pinera, P. et al. (2008) Curr. Opin. Hematol. 15:210.
- Weng, T. and L. Liu (2010) Respir. Res. 11:80.
- Raulo, E. et al. (2005) J. Biol. Chem. 280:41576.
- Hamma-Kourbali, Y. et al. (2008) J. Cell. Physiol. 214:250.
- Lu, K.V. et al. (2005) J. Biol. Chem. 280:16953.
- Yeh, H-J. et al. (1998) J. Neurosci. 18:3699.
- Marchionini, D.M. et al. (2007) Brain Res. 1147:77.
- Chang, Y. et al. (2007) Proc. Natl. Acad. Sci. USA 104:10888.
- Himburg, H.A. et al. (2010) Nat. Med. 16:475.
- Kinnunen, T. et al. (1996) J. Biol. Chem. 271:2243.
- Meng, K. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2603.
- Perez-Pinera, P. et al. (2007) J. Biol. Chem. 282:28683.
- Fukada, M. et al. (2006) FEBS Lett. 580:4051.
- Svensson, S.L. et al. (2010) J. Biol. Chem. 285:16105.
Citations for Recombinant Mouse Pleiotrophin/PTN Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Constitutive Pleiotrophin Deletion Results in a Phenotype with an Altered Pancreatic Morphology and Function in Old Mice
Authors: Ballesteros-Pla, C;Sevillano, J;Sánchez-Alonso, MG;Limones, M;Pita, J;Zapatería, B;Sanz-Cuadrado, MI;Pizarro-Delgado, J;Izquierdo-Lahuerta, A;Medina-Gómez, G;Herradón, G;Ramos-Álvarez, MDP;
International journal of molecular sciences
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay -
Chronic myelogenous leukemia stem cells require cell-autonomous pleiotrophin signaling
Authors: HA Himburg, M Roos, T Fang, Y Zhang, CM Termini, L Schlussel, MM Kim, A Pang, J Kan, L Zhao, H Suh, JP Sasine, G Sapparapu, PM Bowers, G Schiller, JP Chute
J. Clin. Invest., 2020-01-02;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Cell Culture -
Pericyte loss leads to circulatory failure and pleiotrophin depletion causing neuron loss
Authors: AM Nikolakopo, A Montagne, K Kisler, Z Dai, Y Wang, MT Huuskonen, AP Sagare, D Lazic, MD Sweeney, P Kong, M Wang, NC Owens, EJ Lawson, X Xie, Z Zhao, BV Zlokovic
Nat. Neurosci., 2019-06-24;22(7):1089-1098.
Species: Mouse, N/A, Transgenic Mouse
Sample Types: In Vivo, Recombinant Protein, Whole Cells
Applications: Bioassay, ELISA Standard, In Vivo -
The loss of Trps1 suppresses ureteric bud branching because of the activation of TGF-beta signaling.
Authors: Gui T, Sun Y, Gai Z, Shimokado A, Muragaki Y, Zhou G
Dev Biol, 2013-03-26;377(2):415-27.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay
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