Analytical Data
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Gene name
LOLPIB
- Application
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Alternative Names
LOLPIB；Major pollen allergen Lol p 5a
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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
Q40240
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Expression Region
26-307aa
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AA Sequence
ADAGYTPAAAATPATPAATPAAAGGKATTDEQKLLEDVNAGFKAAVAAAANAPPADKFKIFEAAFSESSKGLLATSAAKAPGLIPKLDTAYDVAYKAAEATPEAKYDAFVTALTEALRVIAGALEVHAVKPATEEVLAAKIPTGELQIVDKIDAAFKIAATAANAAPTNDKFTVFESAFNKALNECTGGAYETYKFIPSLEAAVKQAYAATVAAAPEVKYAVFEAALTKAITAMTQAQKAGKPAAAAATAAATVATAAATAAAVLPPPLLVVQSLISLLIYY
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Molecular Weight
35.3 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 LOLP (Late Embryogenesis Abundant Protein) and its recombinant variants has gained significant attention due to the crucial role these proteins play in plant stress responses and developmental processes. LOLP proteins are classified as late embryogenesis abundant proteins, which are typically expressed during the late stages of seed development and under stress conditions, such as drought and salinity. Their ability to protect cellular structures and facilitate cellular hydration makes them of great interest for agricultural biotechnology. With the increasing challenges posed by climate change and food security, there is an urgent need to enhance crop resilience. The study of recombinant LOLP proteins aims to elucidate their mechanisms of function and potential applications in genetically modifying plants to improve stress tolerance. By utilizing techniques such as molecular cloning and protein expression, researchers seek to produce recombinant LOLP proteins for in vitro and in vivo studies, enabling the assessment of their effects on plant growth and stress resistance. Furthermore, understanding the structure-function relationship of these proteins can pave the way for innovative strategies in crop improvement, ultimately contributing to sustainable agriculture. The ongoing exploration of LOLP proteins underscores their significance in plant biology and their potential utility in mitigating the effects of environmental stressors on crop yield.
