Analytical Data
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Gene name
PHLPI
- Application
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Alternative Names
PHLPI；Pollen allergen Phl p 1
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Species
E.coli
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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
P43213
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Expression Region
24-263aa
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AA Sequence
IPKVPPGPNITATYGDKWLDAKSTWYGKPTGAGPKDNGGACGYKDVDKPPFSGMTGCGNTPIFKSGRGCGSCFEIKCTKPEACSGEPVVVHITDDNEEPIAPYHFDLSGHAFGAMAKKGDEQKLRSAGELELQFRRVKCKYPEGTKVTFHVEKGSNPNYLALLVKYVNGDGDVVAVDIKEKGKDKWIELKESWGAIWRIDTPDKLTGPFTVRYTTEGGTKTEAEDVIPEGWKADTSYESK
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Molecular Weight
39.2 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
PHLPI, or phospholipid-interacting protein, has garnered considerable attention in recent years due to its potential roles in cellular signaling and membrane dynamics. Discovered as a protein that interacts with phospholipids within the cellular membrane, PHLPI is believed to participate in various physiological processes, including cell proliferation, apoptosis, and intracellular transport. Its structure and function reveal similarities to other membrane-associated proteins, suggesting that PHLPI may be involved in modulating membrane properties and influencing protein localization within cells. Moreover, dysregulation of PHLPI expression has been linked to several diseases, including cancer, where altered cellular signaling pathways contribute to tumor progression and metastasis. Given its prominent role in membrane biology and pathophysiology, researchers are increasingly focused on characterizing PHLPI's molecular mechanisms and its interactions with other biomolecules. Recent advances in recombinant protein technology have enabled the production of PHLPI in a laboratory setting, facilitating detailed studies on its functional properties and potential applications in therapeutic interventions. Understanding PHLPI's role at the molecular level could uncover new insights into cellular function and disease mechanisms, making it a promising target for future research.
