Analytical Data
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Gene name
LOLPIB
- Application
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Alternative Names
Allergen Lol p Ib Allergen Lol p Va Allergen: Lol p 5a
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Species
Lolium perenne
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q40240
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Expression Region
26-307aa
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Molecular Weight
48.4 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 research on LOLPIB, a recombinant protein, stems from the growing interest in the role of proteins in various biological processes, particularly in the fields of immunology and biotechnology. LOLPIB has been identified for its potential applications in therapeutic interventions due to its unique structural properties and functional capabilities. Recombinant proteins have become invaluable tools in research, allowing scientists to produce proteins that are otherwise difficult to isolate from natural sources. The ability to manipulate genetic sequences in microorganisms enables the large-scale production of LOLPIB, facilitating studies on its interactions and functions. Understanding the mechanisms by which LOLPIB operates could lead to innovations in drug development, vaccine formulation, and disease treatment strategies. As researchers delve deeper into the molecular characteristics and biological activities of LOLPIB, these investigations may uncover significant insights into protein dynamics and their implications in health and disease, thereby contributing to advancements in medical science and therapeutic applications.
