Analytical Data
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Gene name
CRYGN
- Application
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Alternative Names
CRYGN;Gamma-crystallin N
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Species
Human
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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
Q8WXF5
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Expression Region
1-182aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL
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Molecular Weight
23 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
CRYGN, or cryptochrome-encoding gene, has garnered attention in recent years due to its crucial role in various biological processes, including the regulation of circadian rhythms and response to environmental stimuli. As a member of the photoreceptor family, CRYGN has been implicated in the light perception mechanisms in organisms ranging from plants to mammals. The study of recombinant CRYGN proteins has become significant for understanding their structure-function relationships and the molecular mechanisms underlying their photoreceptive capabilities. By expressing CRYGN as a recombinant protein, researchers can elucidate its interaction with light and other cellular components, thereby providing insights into its role in signaling pathways and its potential therapeutic applications. Additionally, the ability to produce large quantities of pure recombinant CRYGN facilitates biochemical assays, structural studies, and the exploration of its evolutionary aspects. These investigations aim not only to enhance our understanding of fundamental biological processes but also to identify potential applications in biotechnology and medicine, such as the development of novel light-responsive systems or the design of drugs targeting circadian rhythm disorders. Overall, research on recombinant CRYGN proteins represents a promising frontier in the intersection of genetics, biochemistry, and applied sciences, potentially leading to significant advancements in both basic and applied research domains.
