Analytical Data
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Gene name
pyp
- Application
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Alternative Names
(PYP)
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Species
Halochromatium salexigens
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P81046
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Expression Region
1-125aa
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Molecular Weight
18.1 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
Related Products
Protein Description
The study of pyridoxal-5'-phosphate (PYP) and its recombinant proteins has gained significant attention in the fields of biochemistry and molecular biology due to their crucial roles in various enzymatic processes and their potential applications in biotechnology. PYP, a derivative of vitamin B6, serves as an important cofactor for numerous enzymes, facilitating critical metabolic reactions. The recombinant production of PYP proteins in model organisms, such as E. coli, allows researchers to investigate their structure-function relationships, stability, and mechanisms of action. Moreover, the generation of these proteins in a controlled environment enhances our ability to explore their biochemical properties in detail. This research is particularly relevant in the context of developing novel therapeutic agents, improving the yield of biotechnological processes, and engineering proteins with enhanced functionalities. By harnessing advanced techniques such as site-directed mutagenesis, researchers aim to create modified PYP proteins that can serve improved roles in industrial applications, medical diagnostics, and treatment strategies. The ongoing exploration of PYP recombinant proteins thus holds great promise for advancing our understanding of enzyme functionality and contributing to innovative solutions in health and industry.
