Analytical Data
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Gene name
SUGP1
- Application
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Alternative Names
SF4
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IWZ8-1
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Expression Region
E169-K243
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Protein Length
Partial
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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
SUGP1 (Surveillance of G1 to S phase Transition 1) is a protein that plays a critical role in various cellular processes, including the regulation of the cell cycle and the response to DNA damage. Its importance arises from its involvement in the surveillance mechanism that ensures the integrity of genetic material during cell division. Dysregulation of SUGP1 has been implicated in several diseases, including cancer, where altered cell cycle progression contributes to tumorigenesis. Recent studies have highlighted SUGP1’s functions in post-transcriptional regulation and its potential as a therapeutic target. Research on the recombinant production of SUGP1 has gained traction due to the need for purified and functional protein for structural and biochemical studies. By engineering bacterial or eukaryotic systems to express SUGP1, scientists aim to investigate its molecular interactions, regulatory pathways, and effects on cellular physiology. Understanding SUGP1 at a molecular level could provide insights into the mechanisms of diseases and aid in the development of novel therapeutic strategies.
