Analytical Data
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Gene name
PHLPI
- Application
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Alternative Names
Allergen Phl p I Allergen: Phl p 1
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Species
Phleum pratense
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Source
E. coli
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Tag
N- His-SUMO
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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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Molecular Weight
42.2 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 (Phospholipid-Protein Interactions) is a significant area of research given its critical role in various biological processes, including cell signaling, membrane dynamics, and protein function. Research on PHLPI recombinant proteins has gained momentum due to their potential applications in drug development, synthetic biology, and understanding disease mechanisms. As cells utilize phospholipids to create membranes and facilitate protein interactions, studying these recombinant proteins can elucidate how proteins associate with lipid membranes, influencing cellular function. Furthermore, such studies contribute to the design of biomimetic systems and lipid-based drug delivery methods, enhancing therapeutic efficacy and specificity. The enhanced understanding of PHLPI through recombinant proteins also provides insights into various pathologies, including cancer and neurodegenerative diseases, where membrane protein interactions are disrupted. Consequently, this research not only advances our fundamental understanding of cellular biology but also opens pathways for innovative therapeutic strategies.
