Analytical Data
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Gene name
PTN
- Application
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Alternative Names
PTN；HBNF1；NEGF1；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
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Protein Description
PTN (Pleiotrophin) is a heparin-binding growth factor that plays a pivotal role in various biological processes, including cell proliferation, differentiation, and survival. Initially identified as a protein influencing neuronal development, PTN has garnered significant attention due to its diverse functions in both the central nervous system and peripheral tissues. Research indicates that PTN is implicated in pathological conditions such as cancer, where it can promote tumor growth and angiogenesis, as well as in regenerative medicine, where it can enhance tissue repair and regeneration. The ability to manipulate PTN expression and activity through recombinant protein technology has opened new avenues for therapeutic interventions. Scientists are actively exploring the structure and function of PTN to develop targeted treatments for diseases linked to dysregulated PTN signaling. Additionally, understanding PTN's interaction with its receptors and extracellular matrix components is critical for elucidating its role in health and disease. The recombinant expression of PTN allows for detailed studies of its biological effects and potential applications in biomedicine, driving research into novel diagnostic and therapeutic strategies.
