Analytical Data
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Gene name
PR-10
- Application
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Alternative Names
PR-10；KIAA1231；PFM7；TRIS；PR domain zinc finger Protein 10
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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
P26987
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Expression Region
1-158aa
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AA Sequence
MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLHKIESIDEANLGYSYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAKADALFKAIEAYLLAHPDYN
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Molecular Weight
18.8 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
PR-10 proteins, belonging to the pathogenesis-related (PR) protein group, are primarily associated with plant defense mechanisms against biotic and abiotic stressors. These proteins were first identified in plants like tobacco and wheat, where they exhibit significant expression levels in response to various environmental challenges, such as pathogen attacks or extreme temperatures. Their role in plant defense is attributed to their ability to possess ribonuclease and antimicrobial activities, enhancing the resistance of plants to pathogens. The study of PR-10 proteins has gained momentum due to their potential applications in agriculture and biotechnology, particularly in developing disease-resistant crop varieties and understanding plant immunity at a molecular level. Moreover, the structural properties of PR-10 proteins, which often exhibit a stable fold conducive to various functions, have made them a subject of interest for recombinant protein engineering. This research aims to explore the functional versatility of PR-10 proteins, including their potential for use in pharmaceuticals and biocontrol agents, tapping into their inherent properties to create innovative solutions for challenges in crop production and plant health management. As agricultural practices evolve in the face of climate change and increasing pest resistance, understanding and harnessing PR-10 proteins could provide critical insights and tools for sustainable agriculture.
