Analytical Data
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Gene name
HSP18.1
- Application
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Alternative Names
HSP 18.1
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Species
Pisum sativum
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19243
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Expression Region
1-158aa
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Molecular Weight
34.1 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
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Protein Description
HSP18.1, a member of the heat shock protein family, is a small molecular chaperone predominantly found in plant cells, particularly in chloroplasts. Its primary function is to assist in protein folding, protect against stress-induced denaturation, and facilitate recovery from heat stress. The significance of HSP18.1 has garnered attention in recent years due to its pivotal role in plant responses to environmental stresses, such as high temperatures and oxidative damage. Research has shown that HSP18.1 not only helps maintain cellular protein integrity under stress conditions but also plays a crucial role in enhancing plant tolerance to various abiotic stresses, thereby influencing growth and yield. Studies have employed recombinant DNA technology to produce HSP18.1 in heterologous systems, allowing for detailed investigations into its functional properties and applications in agricultural biotechnology. Understanding the molecular mechanisms underlying HSP18.1's functions could lead to innovative strategies for improving stress resilience in crops. As global climate change increasingly threatens agricultural productivity, the study of HSP18.1 and its recombinant protein forms holds promising potential for developing resilient plant varieties capable of withstanding extreme environmental challenges.
