Analytical Data
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Gene name
PHLPVI
- Application
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Alternative Names
Allergen Phl p VI;Phl p 6
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Species
Phleum pratense
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Source
E. coli
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Tag
N- His & C- Myc
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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
23-132aa
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Molecular Weight
19.2 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
PHLPVI (PH domain and leucine-rich repeat protein 1) is a protein of significant interest due to its potential roles in various cellular processes and disease mechanisms. Research on PHLPVI has gained traction as studies have indicated its involvement in regulating signaling pathways linked to cell growth, differentiation, and apoptosis. Its unique structural characteristics, featuring a PH domain and leucine-rich repeats, suggest that PHLPVI may mediate protein-protein interactions and cellular signaling networks. Additionally, emerging evidence suggests that dysregulation of PHLPVI expression may be associated with several pathological conditions, including cancer and neurodegenerative diseases. Investigating PHLPVI as a recombinant protein provides the opportunity to elucidate its functional properties, interaction partners, and the mechanisms by which it influences cellular behavior. Recombinant techniques allow for the production of PHLPVI in sufficient quantities for detailed biophysical analyses and functional assays, facilitating a deeper understanding of its role in health and disease. As research advances, PHLPVI may emerge as a potential biomarker or therapeutic target, highlighting the importance of understanding its biochemical characteristics and biological implications.
