Analytical Data
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Gene name
CREB
- Application
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Alternative Names
CREB1; CAMP Responsive Element Binding Protein 1
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Species
Human
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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
P16220
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Expression Region
Ile102~Asp341
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Molecular Weight
36kDa
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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
CREB, or cAMP response element-binding protein, is a crucial transcription factor that plays a significant role in cellular signaling and gene expression regulation. It is activated in response to various extracellular signals, such as hormones and neurotransmitters, which trigger intracellular signaling cascades leading to increased levels of cyclic AMP (cAMP). Once phosphorylated, CREB binds to specific DNA sequences known as cAMP response elements (CREs) to initiate the transcription of target genes involved in essential processes like neuronal plasticity, survival, metabolism, and cell proliferation. The dysregulation of CREB activity has been implicated in numerous diseases, including neurological disorders, cancer, and metabolic syndromes, making it a key focus of biomedical research. Researchers are particularly interested in CREB fusion proteins, which can be engineered to enhance understanding of CREB's functional roles in various cellular contexts. These reconstituted CREB proteins can serve as valuable tools for investigating the molecular mechanisms underlying CREB-mediated transcriptional regulation, identifying potential therapeutic targets, and exploring the pathways involved in disease processes. Thus, the study of CREB recombination proteins not only deepens our understanding of fundamental biological processes but also holds promise for developing innovative strategies in disease treatment and prevention.
