Analytical Data
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Gene name
CRYbB1
- Application
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9WVJ5
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Expression Region
Lys6~Val186
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Molecular Weight
50kDa
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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
CRYbB1, a member of the cryptochrome family, plays a crucial role in regulating circadian rhythms and various light-responsive processes in plants. As a blue light receptor, CRYbB1 is involved in the physiological adaptation of plants to their environment, influencing growth, development, and stress responses. Research on CRYbB1 recombinant protein is motivated by its potential applications in agriculture and biotechnology. Understanding the structure-function relationship of CRYbB1 can provide insights into its signaling mechanisms and interactions with other proteins. This knowledge could lead to the development of genetically modified crops with enhanced resilience to environmental stressors or improved yields under varying light conditions. Furthermore, studying the recombinant protein may facilitate the exploration of its involvement in photomorphogenesis and photoperiodism, making it a valuable target for further functional studies. Overall, the investigation of CRYbB1 recombinant protein is essential for unraveling the complexities of plant responses to light, potentially contributing to innovative agricultural strategies in the face of climate change.
