Human Pleiotrophin is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Specifications for Human Pleiotrophin

Overview

Human Pleiotrophin is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Applications

Human Pleiotrophin can be used for a variety of applications, including:
  • Study of neuronal development.
  • Study of PTP-zeta and anaplasic lymphoma kinase.
  • Cancer research.

Detailed product information

Background information

Pleiotrophin (PTN) is a heparin-binding non-glycosylated growth factor containing 136 amino acids. The protein is mainly found in tissue of the central nervous system. The concentration of Pleiotrophin reaches its’ peak in the late fetal state and is maintained in later stages of life. Pleiotrophin is thought to play a role in the growth and the maturation of the brain. If applied to neurons in cell culture it supports the growth of neurites. It was also suggested that Pleiotrophin might play a role in the pathogenesis of neuroblastomas.

Quality description

Research-grade
cytokines are suitable for a wide variety of cell culture applications. They are sterile-filtered prior to lyophilization. Generally, endotoxin levels are <0.1 ng/μg (<1 EU/μg), and purities are >95%. The biological activity is tested in appropriate bioassays.

Resources for Human Pleiotrophin

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for Human Pleiotrophin

Publications

  1. Böhlen, P and Kovesdi, I. (1991) HBNF and MK, members of a novel gene family of heparin-binding proteins with potential roles in embryogenesis and brain function. PLoS Negl Trop Dis. 3: 143-157
  2. Bloch, B. et al. (1992) Expression of the HBNF (heparin-binding neurite-promoting factor) gene in the brain of fetal, neonatal and adult rat: an in situ hybridization study. Brain Res. Mol. Brain Res. 70: 267-278
  3. Chauhan, AK. et al. (1993) Pleiotrophin transforms NIH 3T3 cells and induces tumors in nude mice. Proc. Natl. Acad. Sci. U.S.A. 90: 679-682
  4. Lai, S. et al. (1992) Structure of the human heparin-binding growth factor gene pleiotrophin. Biochem. Biophys. Res. Commun. 187: 1113-1122
  5. Naito, A. et al. (1992) Similarity of the genomic structure between the two members in a new family of heparin-binding factors. Biochem. Biophys. Res. Commun. 183: 701-777
  6. Raulo, E. et al. (1994) Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). J. Biol. Chem. 269(17): 12999-13004
  7. Wanaka, A. et al. (1993) Developmentally regulated expression of pleiotrophin, a novel heparin binding growth factor, in the nervous system of the rat. Brain Res. Mol. Brain Res. 72: 133-144

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