Analytical Data
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Gene name
CUP1-1
- Application
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Alternative Names
CUP1-1；ACE1；Transcriptional activator Protein CUP2
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Species
E.coli
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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
P0CX80
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Expression Region
9-61aa
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AA Sequence
QNEGHECQCQCGSCKNNEQCQKSCSCPTGCNSDDKCPCGNKSEETKKSCCSGK
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Molecular Weight
32.3 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
CUP1-1, a copper-binding protein found in yeast, serves as a pivotal model for understanding metal homeostasis and stress responses in eukaryotic cells. Its study is rooted in the increasing recognition of the role of metalloproteins in cellular functions and their implications in health and disease. The expression of CUP1-1 is primarily induced by copper exposure, acting as a critical mechanism for detoxifying excess copper and maintaining cellular metal balance. Additionally, CUP1-1 has garnered interest due to its involvement in processes such as oxidative stress response, which is relevant in the context of aging and various neurodegenerative diseases. Researchers have been investigating the structure, function, and regulatory mechanisms of CUP1-1 to elucidate how it coordinates with cellular pathways to mitigate metal toxicity and to explore its potential applications in biotechnology, particularly in bio-remediation and the development of biosensors. Furthermore, as a model system in yeast, studies of CUP1-1 effectively bridge fundamental biological research with practical applications, emphasizing the importance of heavy metal management in living organisms and the environmental implications of metal exposure.
