Analytical Data
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Gene name
dSIP
- Application
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Alternative Names
dSIP；DSIPI；GILZ；TSC22 domain family Protein 3
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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
Q99576
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Expression Region
1-134aa
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AA Sequence
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI DNKIEQAMDL VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SCLSPEEPAP ESPQVPEAPG GSAV
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Molecular Weight
14.8 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
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Protein Description
dSIP (dormant site protein) is a recombinant protein that has garnered significant interest due to its potential role in cellular stress responses and developmental processes. Research indicates that dSIP is involved in regulating sleep and circadian rhythms, offering insights into its function as a key player in the endocrine and nervous systems of various organisms. Initial studies have suggested that dSIP may interact with other proteins and cellular pathways, highlighting its importance in maintaining homeostasis during environmental challenges. The ability to produce dSIP as a recombinant protein has allowed for the exploration of its structure-function relationships, facilitating in vitro studies that aim to uncover its mechanistic roles. Moreover, understanding the regulation of dSIP expression and its functional implications is crucial for addressing sleep disorders and metabolic diseases, making it a promising target for therapeutic interventions. As such, the ongoing research into dSIP not only contributes to our fundamental understanding of biological processes but also opens avenues for potential clinical applications.
