Analytical Data
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Gene name
PHLPVI
- Application
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Alternative Names
PHLPVI；Pollen allergen Phl p 6
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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
P43215
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Expression Region
1-132aa
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AA Sequence
MVAMFLAVAVVLGLATSPTAEGGKATTEEQKLIEDVNASFRAAMATTANVPPADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYNAADHAAPEDKYEAFVLHFSEALRIIAGTPEVHAVKPGA
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Molecular Weight
13.9 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
The study of PHLPVI (PH domain and Leucine-rich repeat Protein 1 Variant I) recombinant protein emerges from the growing interest in understanding the biological roles and mechanisms of proteins that contain PH domains and leucine-rich repeats. PHLPVI has gained attention due to its potential involvement in cellular signaling pathways and disease processes, including cancer and neurodegenerative disorders. Previous research suggests that proteins with similar structural motifs play critical roles in mediating protein-protein interactions and cellular localization, which are vital for maintaining cellular homeostasis. The recombinant expression of PHLPVI enables researchers to produce substantial quantities of the protein for functional studies and characterization. Utilizing techniques such as molecular cloning, expression in suitable host systems, and purification methods, scientists can investigate the biochemical properties, structural characteristics, and biological activities of PHLPVI. Understanding the functional implications of PHLPVI at the molecular level may provide insights into its role in health and disease, paving the way for potential therapeutic applications. As the field continues to evolve, ongoing studies focus on elucidating the specific interactions and pathways mediated by PHLPVI, thereby contributing to a deeper understanding of its significance in various physiological and pathological contexts.
