Recombinant Rat Pleiotrophin (PTN) Protein (His)

Name: Recombinant Rat Pleiotrophin (PTN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06972P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Rat Pleiotrophin (PTN) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P63090
Target Symbol	PTN
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNADCQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD
Expression Range	33-168aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.4 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups. Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone. Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation. Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK or AFAP1L2 in order to activate the PI3K-AKT pathway. Through PTPRZ1 binding, regulates endothelial cell migration and controls oligodendrocyte precursor cell differentiation. Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation. In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway. Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion. Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition. Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation. Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway. Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration. In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway.
Subcellular Location	Secreted.
Protein Families	Pleiotrophin family
Database References	KEGG: rno:24924 STRING: 10116.ENSRNOP00000016088 UniGene: Rn.1653
Tissue Specificity	Expressed in brain. Hardly expressed in bone. Abundantly expressed in the growth plate. Intensely expressed in the cartilage matrix that forms the hollow for the secondary ossification center. Is expressed selectively by the osteocytes of the lamellar bon

Gene Functions References

PTN and RPTPbeta/zeta are expressed in spinal deformities caused by mechanical loading, and their expression depends on the type and severity of the applied strain. PMID: 26615567
Pleiotrophin is a novel genetic factor that plays a role in morphine withdrawal syndrome. PMID: 26222257
We hypothesize a role for these cytokines in mediating, at least in part, acute neuroprotective effects and chronic neurotrophic adaptations that contribute to drug dependence. PMID: 25108770
These findings provide new insight into the neuroprotective role of PTN PMID: 23000062
PTN significantly prevented glutamate-induced neurotoxicity of cultured hippocampal neurons. PMID: 21928404
(HARP)/pleiotrophin, a cytokine known to regulate developmental chondrocyte formation, were enhanced especially at 4 weeks, without up-regulation of HARP/pleiotrophin mRNA in overuse tendon injury. PMID: 21688311
pleiotrophin expression in rat liver PMID: 11999218
PTN is secreted from activated adult hepatic stellate cells and embryonic mesenchymal cells as a mitogen of parenchymal cells in adult and embryonic liver, respectively. PMID: 12057922
that PTN is up-regulated in DA-depleted striatum and exhibits a trophic effect specifically on the survival of cultured dopaminergic neurons. PMID: 12786979
Using immunohistochemical techniques we could show that PTN is expressed in fracture callus, while this angiogenic peptide was undetectable in normal bone. PMID: 14586627
PTN signals new blood vessel formation through its ability to stimulate different functions in different cell types not limited to the endothelial cell PMID: 15949466
thrombospondin type I repeat domains of the heparin-binding growth-associated molecule bind to heparin/heparan sulfate and regulate neurite extension and plasticity in hippocampal neurons PMID: 16155004
hypoxia and platelet-derived growth factor mediated induction of PTN expression in sinusoidal hepatic stellate cells may provide a strong mitogenic signal for hepatocytes to limit the damage to the parenchymal cells in biliary-type liver fibrogenesis PMID: 16226713
PTN-immunolabeled neurons contained nitric oxide synthase or somatostatin and expressed the vesicular acetylcholine transporter, supporting that they were GABAergic nitric oxide synthase/somatostatin-containing and cholinergic interneurons PMID: 16325783
Together, these results demonstrate that influence of CNTF family of cytokines on the differentiation of late retinal progenitor cell population is partially mediated by the release of Ptn. PMID: 16914133
Pleiotrophin is a neurotrophic factor for spinal motor neurons PMID: 17360581
PTN was identified as a factor that plays a role in the nigrostriatal system during development and in response to disease, and may therefore be useful for neuroprotection or reconstruction of the dopamine system PMID: 17368428
HARP negatively affects diverse biological activities in C6 glioma cells, mainly due to binding of HARP to VEGF, which may sequester secreted VEGF from signalling through VEGFR2. PMID: 17881084
upregulation of PTN, but not MK, could play an important role in the recovery from nerve damage PMID: 18365878
pleiotrophin (PTN) and syndecan-2 and -3 as direct binding partners of Y-P30. PMID: 18599487
Pleiotrophin prevents cocaine-induced toxicity in vitro. PMID: 18727926
PTN inhibits hippocampal LTP in vitro and might play a role in memory processes in vivo. PMID: 19384682

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.