Recombinant Mouse Pleiotrophin/PTN Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Pleiotrophin/PTN Protein, CF Summary

Details of Functionality
Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cerebral cortical neurons. Muramatsu, H. and T. Muramatsu (1991) Biochem. Biophys. Res. Commu. 177:652. Optimal neurite outgrowth was observed when neurons were plated on 96 well culture plates that had been pre-coated with 100 µL/well of recombinant mouse Pleiotrophin at 3‑8 µg/mL.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse Pleiotrophin/PTN protein
Met1-Asp168
Accession #
N-terminal Sequence
Gly33
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
15.3 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
19 kDa, reducing conditions
Publications
Read Publications using
6580-PL in the following applications:

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.
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 Mouse Pleiotrophin/PTN Protein, CF

  • HARP
  • HBBM
  • HB-GAM
  • HBGF8
  • HBNF
  • HBNF1
  • HBNF-1
  • Heparin-binding brain mitogen
  • HNGF-8
  • NEGF1HBGF-8
  • neurite growth-promoting factor 1
  • neurite growth-promoting factor1)
  • OSF-1
  • Osteoblast-specific factor 1
  • Pleiotrophin
  • PTN

Background

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).

  1. Naito, A. et al. (1992) Biochem. Biophys. Res. Commun. 183:701.
  2. Perez-Pinera, P. et al. (2008) Curr. Opin. Hematol. 15:210.
  3. Weng, T. and L. Liu (2010) Respir. Res. 11:80.
  4. Raulo, E. et al. (2005) J. Biol. Chem. 280:41576.
  5. Hamma-Kourbali, Y. et al. (2008) J. Cell. Physiol. 214:250.
  6. Lu, K.V. et al. (2005) J. Biol. Chem. 280:16953.
  7. Yeh, H-J. et al. (1998) J. Neurosci. 18:3699.
  8. Marchionini, D.M. et al. (2007) Brain Res. 1147:77.
  9. Chang, Y. et al. (2007) Proc. Natl. Acad. Sci. USA 104:10888.
  10. Himburg, H.A. et al. (2010) Nat. Med. 16:475.
  11. Kinnunen, T. et al. (1996) J. Biol. Chem. 271:2243.
  12. Meng, K. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2603.
  13. Perez-Pinera, P. et al. (2007) J. Biol. Chem. 282:28683.
  14. Fukada, M. et al. (2006) FEBS Lett. 580:4051.
  15. Svensson, S.L. et al. (2010) J. Biol. Chem. 285:16105.

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Publications for Pleiotrophin/PTN (6580-PL)(2)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 2 applications: Bioassay, Cell Culture.


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(1)
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