| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | PTN |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. For long-term storage of diluted solutions, we recommend adding 0.1% BSA. Repeat freeze-thawing may result in loss of activity. |
| Source | Recombinant, E. coli |
| Storage | |
| Target |
Overview
Recombinant human Pleiotrophin protein is a research-grade protein/peptide reagent used in research settings. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows.
Key elements and design rationale
- Molecular identity: MW: 15.4 kDa.
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
Pleiotrophin (PTN), is a heparin-binding neurotrophic factor. Cells that express either PTN or PTN mRNA include osteoblasts, fetal chondrocytes,1 astrocytes, oligodendroglia, neurons,2 Schwann cells,3 keratinocytes of the stratum basale,3 and selected tumor cell lines.4,5 The expression of PTN increases during the process of brain embryogenesis and reaches maximum levels at time of birth.The role of PTN in neurogenesis and neural plasticity has been revealed by various studies. Embryonic cortical neurons adhere to and extend neurites on PTN coated substratuM6 PTN also induces, in vitro, migration of osteoblasts. 7 PTN coated membrane enhances neuronal migration by haptotaxis.8 PTN bound to agarose beads induces clustering of acetylcholine receptors on embryonic myoblasts.9PTN is expressed in the CA1 region of rat hippocampus in an activity-dependent manner, and is suggested to be involved in the regulation of synaptic plasticity in the hippocampus.10Transfection with PTN cDNA, transforms murine 3T3 fibroblasts into cells that form extensively metastasizing tumors in nude mice.11 PTN is highly expressed in choriocarcinoma, melanoma and, prostate carcinoma. Serum PTN increase in patients with pancreatic and colon carcinomas.12After focal forebrain ischemia, PTN is expressed in astrocytes, OX-42 positive macrophages, and endothelial cells in areas of developing neovascularization.13 PTN is also deposited in senile plaques in Alzheimer's disease and Down's syndrome.14
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Assay development and optimization: used as a reference material or tool reagent in RUO workflows.
- Reagent validation: supports conceptual controls such as competition/neutralization, when relevant.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Desaphy, J. F.
et al. (2010) Br. J. Pharmacol.160, 1521.
Nakagawara, A.
et al. (1995) Cancer Res. 55, 1792.
Kuo, M.D.
et al. (1992) Biochem. Biophys. Res. Commun. 182, 188.
Raulo, E.
et al. (1994) J. Biol. Chem. 269, 12999.
Mitsiadis, T.A.
et al. (1995) Development 121, 37.
Rauvala, H.
(1989) EMBO. J. 8, 2933.
Imai, S.
et al. (1998) J. Cell Biol. 143, 1113.
Maeda, N.
et al. (1998) J. Cell Biol. 142, 203.
Peng, H.B.
et al. (1995) J. Neurosci. 15, 3027.
Lauri, S.E.
et al. (1998) Eur. J. Neurosci. 10, 188.
Chauhan, A.K.
et al. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 679.
Souttou, B.
et al. (1998) J. Natl. Cancer Inst. 90, 1468.
Yeh, H.J.
et al. (1998) J. Neurosci. 18, 3699.
Wisniewski, T.
et al. (1996) Neuroreport 7, 667.
Wisniewski, T.
et al. (1996) Neuroreport 7, 667.
Garver, R.I.
et al. (1994) Cancer 74, 1584.
Li, Y.S.
et al. (1990) Science 250, 1690.
Asai, T.
et al. (1997) Biochem. Biophys. Res. Commun. 236, 60.
Owada, K.
et al. (1999) J. Neurochem. 73, 2084.
Owada, K.
et al. (1999) J. Neurochem. 73, 2084.