Recombinant Human 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 a solution of 3‑8 µg/mL rhPTN.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Pleiotrophin/PTN protein Gly33-Asp168
>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
Bioactivity
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
18 kDa, reducing conditions
Publications
Read Publications using 252-PL in the following applications:
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
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human 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
PTN was identified independently by several groups as a novel heparin-binding, developmentally regulated cytokine. Depending on the biological activities studied, this protein has variously been referred to as heparin-binding brain mitogen (HBBM), heparin-binding growth factor-8 (HBGF-8), heparin-binding neurite promoting factor, heparin-binding neurotrophic factor (HBNF), heparin-affinity regulatory peptide (HARP), heparin-binding growth-associated molecule (HB-GAM), osteoblast-specific factor (OSF-1), and pleiotrophin. PTN is a highly conserved protein; the amino acid sequences of human, bovine, rat, and mouse PTN share > 98% homology.
PTN is a member of a family of heparin-binding proteins that share sequence, structural, and functional similarity. Other members of this family include midkine (MK), and chicken retinoic acid-induced heparin-binding protein (RI-HB), an avian homologue of MK. The expression of all these cytokines is restricted and highly regulated during development.
PTN can be used as an attachment substrate to stimulate neurite outgrowth in mixed cultures of embryonic rat, mouse or chicken brain cells. Although both natural and recombinant human PTN have been reported to be mitogenic for fibroblasts, endothelial, and epithelial cells, the data are still highly controversial. The insect cell-derived recombinant PTN preparations produced at R&D Systems lack mitogenic activities when tested on various fibroblast, endothelial, and epithelial cell lines. PTN has been shown to transform NIH-3T3 and SW-13 cells, as evidenced by anchorage-independent growth and tumor formation in the nude mouse. These results suggest that, in spite of the conflicting reports of PTN’s growth-promoting activity in vitro, PTN may have a role in abnormal cell growth in vivo.
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