Analytical Data
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Gene name
phr
- Application
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Alternative Names
phr；KIAA1733；RPEL1；Phosphatase and actin regulator 1
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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
P05327
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Expression Region
2-484aa
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AA Sequence
AAPILFWHRRDLRLSDNIGLAAARAQSAQLIGLFCLDPQILQSADMAPARVAYLQGCLQELQQRYQQAGSRLLLLQGDPQHLIPQLAQQLQAEAVYWNQDIEPYGRDRDGQVAAALKTAGIRAVQLWDQLLHSPDQILSGSGNPYSVYGPFWKNWQAQPKPTPVATPTELVDLSPEQLTAIAPLLLSELPTLKQLGFDWDGGFPVEPGETAAIARLQEFCDRAIADYDPQRNFPAEAGTSGLSPALKFGAIGIRQAWRAASAAHALSRSDEARNSIRVWQQELAWREFYQHALYHFPSLADGPYRSLWQQFPWENREALFTAWTQAQTGYPIVDAAMRQLTETGWMHNRCWMIVASFLTKDLIIDWRRGEQFFMQHLVDGDLAANNGGWQWSASSGMDPKPLRIFNPASQAKKFDATATYIKRWLPELRHVHPKDLISGEITPIGRRGYPAPIVNHNLRQKQFKALYNQLKAAIAEPEAEPDS
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Molecular Weight
74.3 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
PHR (Phototropic Helix Repeats) recombinant proteins have garnered significant attention in recent years due to their unique structural and functional properties. These proteins, characterized by their ability to respond to light stimuli, play crucial roles in various biological processes, including phototropism and light signal transduction in plants. With advancements in molecular biology techniques, researchers have been able to isolate and recombinantly express PHR proteins, allowing for detailed studies of their mechanisms and interactions. Understanding the role of PHR proteins not only provides insights into plant biology but also opens avenues for biotechnological applications, such as developing crops with enhanced growth patterns in varying light conditions and engineering novel protein-based systems for optogenetics. Additionally, the study of PHR proteins contributes to the broader field of protein engineering, where the manipulation of their properties can lead to innovative solutions in synthetic biology and materials science. Through ongoing research, the potential for harnessing PHR proteins in both fundamental and applied sciences continues to expand, highlighting their importance in the intersection of biology and technology.
