Analytical Data
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Gene name
CRYbA1
- Application
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Alternative Names
CRYB1; Eye Lens Structural Protein
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Species
Mouse
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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
P02525
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Expression Region
Met1~Gln215
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Molecular Weight
29kDa
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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
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Protein Description
CRYbA1 is a unique photoreceptor protein that belongs to the cryptochrome family, which plays a crucial role in the regulation of circadian rhythms and various physiological processes. Originating from specific plant and animal species, research on CRYbA1 has gained significant attention due to its potential applications in understanding light signaling pathways and their impact on biological functions. Recent advancements in molecular biology techniques have enabled scientists to express and purify CRYbA1 as a recombinant protein, facilitating in-depth studies of its structure and function. Investigations have revealed the interaction of CRYbA1 with other cellular components and its role in modulating gene expression in response to light stimuli. The ability to produce large quantities of CRYbA1 in a laboratory setting enhances the potential for biochemical assays, structural biology studies, and drug discovery efforts targeting circadian rhythm-related disorders. Moreover, elucidating the mechanisms by which CRYbA1 functions could contribute to the development of novel strategies for improving crop yields and resilience in plants. As a result, CRYbA1 recombinant protein studies are not only pivotal for fundamental research but also hold significant promise for practical applications in agriculture and medicine. The ongoing exploration of CRYbA1 highlights the intricate relationship between light and biological systems, underscoring the importance of this protein in advancing our understanding of circadian biology and its relevance to health and sustainability.
