Analytical Data
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Gene name
PRO1
- Application
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Alternative Names
Pollen allergen Cyn d 12 Allergen: Cyn d 12
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Species
Cynodon dactylon
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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
O04725
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Expression Region
2-131aa
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Molecular Weight
30 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
PRO1 is a recombinant protein that has gained significant attention in recent years due to its potential applications in various fields, including biotechnology, pharmaceuticals, and molecular biology. The study of PRO1 is rooted in the need for understanding protein folding, stability, and functionality, as well as the development of novel therapeutic agents. As recombinant DNA technology has advanced, the ability to produce proteins in heterologous systems, such as bacteria, yeast, or mammalian cells, has enabled researchers to obtain large quantities of PRO1 for detailed study. Investigations into PRO1’s structure-function relationship have revealed insights into its biological role and interactions, paving the way for its use in drug design, vaccine formulation, and diagnostic applications. Furthermore, the challenges associated with the expression and purification of PRO1 have led to the exploration of innovative biotechnological approaches, such as fusion proteins and targeted mutagenesis, to enhance yield and functionality. Overall, the research on PRO1 not only contributes to our understanding of protein chemistry but also opens new avenues for developing biotherapeutics and bioprocessing technologies.
