Analytical Data
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Gene name
PTN
- Application
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Alternative Names
PTN；HBNF1；Pleiotrophin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21246
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Expression Region
33-168aa
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AA Sequence
MGKKEKPEKK VKKSDCGEWQ WSVCVPTSGD CGLGTREGTR TGAECKQTMK TQRCKIPCNW KKQFGAECKY QFQAWGECDL NTALKTRTGS LKRALHNAEC QKTVTISKPC GKLTKPKPQA ESKKKKKEGK KQEKMLD
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Molecular Weight
19 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PTN (Pleiotrophin) is a heparin-binding growth factor known for its diverse biological functions, including roles in neurodevelopment, angiogenesis, and tissue repair. Research into PTN began with its initial discovery as a key player in promoting neuronal differentiation and growth in the nervous system. As studies progressed, PTN was found to be involved in various disease processes, including cancer, where it may contribute to tumor growth and metastasis by enhancing angiogenic pathways. Furthermore, PTN has been implicated in the regulation of cellular interactions through its binding to specific receptors and extracellular matrix components. The exploration of PTN as a recombinant protein has gained traction due to its potential therapeutic applications, particularly in regenerative medicine and oncology. By harnessing PTN's biological properties, researchers aim to develop novel treatments that could leverage its ability to promote cell proliferation, migration, and survival in damaged tissues. Additionally, understanding the structure-function relationship of PTN at the molecular level is critical for designing effective biomolecules that can modulate its activity and enhance its therapeutic efficacy. Overall, the study of PTN and its recombinant forms is essential for uncovering new strategies in the treatment of neurodegenerative diseases, cardiovascular disorders, and various cancers.
