Analytical Data
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Gene name
PYL1
- Application
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Alternative Names
PYL1；RCAR12；Abscisic acid receptor PYL1
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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
Q8VZS8
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Expression Region
8-221aa
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AA Sequence
SSPVNEEENSQRISTLHHQTMPSDLTQDEFTQLSQSIAEFHTYQLGNGRCSSLLAQRIHAPPETVWSVVRRFDRPQIYKHFIKSCNVSEDFEMRVGCTRDVNVISGLPANTSRERLDLLDDDRRVTGFSITGGEHRLRNYKSVTTVHRFEKEEEEERIWTVVLESYVVDVPEGNSEEDTRLFADTVIRLNLQKLASITEAMNRNNNNNNSSQVR
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Molecular Weight
28.7 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
PYL1 protein, a pivotal component in the abscisic acid (ABA) signaling pathway, plays a critical role in plant stress responses, particularly under drought and salinity conditions. This protein acts as a receptor for ABA, facilitating the transmission of stress signals that contribute to various physiological processes such as stomatal closure, seed germination, and overall plant growth regulation. Research on PYL1 has garnered significant attention due to its potential applications in enhancing plant resilience to environmental stresses, which is increasingly vital in the context of global climate change and food security challenges. By understanding the molecular mechanisms through which PYL1 operates, scientists aim to develop crops that can better withstand adverse conditions, ensuring stable yields in our changing environment. Advances in recombinant protein production techniques have enabled the detailed study of PYL1's structure and function, contributing to the development of targeted genetic engineering approaches for crop improvement. Thus, PYL1 research not only deepens our understanding of plant biology but also holds promise for sustainable agricultural practices in the face of rising environmental challenges.
