Analytical Data
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Gene name
chain
- Application
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Alternative Names
Phosphatidylcholine 2-acylhydrolase
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Species
Pseudechis porphyriacus
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Source
Yeast
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Tag
N- His-sumostar
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20259
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Expression Region
1-117aa
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Molecular Weight
29 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
Chain recombinant proteins, which are generated through the fusion of specific genes and the subsequent expression in host organisms, have emerged as crucial tools in biotechnology and medicine. The advent of genetic engineering techniques has enabled researchers to manipulate the DNA sequences encoding proteins, allowing for the production of proteins with enhanced properties, such as improved solubility, stability, or activity. The significance of chain recombinant proteins lies in their applications across various fields, including therapeutic development, vaccine production, and enzyme engineering. In biopharmaceuticals, for instance, recombinant proteins are essential for developing monoclonal antibodies and other biologics, providing targeted therapies for diseases like cancer and autoimmune disorders. The ability to produce these proteins in organisms such as bacteria, yeast, and mammalian cells has revolutionized the pharmaceutical industry, offering a more efficient and scalable approach compared to traditional methods of protein extraction from natural sources. Furthermore, chain recombinant proteins are pivotal in advancing fundamental research, as they facilitate the study of protein function, interactions, and structure. Thus, ongoing research in the design, expression, and purification of chain recombinant proteins continues to enhance our understanding of biological processes and contributes to innovations in therapeutic solutions.
