Analytical Data
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Gene name
CREBL2
- Application
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Alternative Names
CREBL2cAMP-responsive element-binding protein-like 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60519
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Expression Region
1-120aa
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AA Sequence
MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIKALLTGEEQNKSQQNSSRHTKAGKTDANSNSW
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Molecular Weight
40.2 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
CREBL2, a member of the CREB (cAMP response element-binding protein) family, has garnered attention in recent years due to its potential roles in various cellular processes, including gene regulation, cell proliferation, and differentiation. Research indicates that CREBL2 may be involved in the response to stress and in the modulation of metabolic pathways, making it an important target in understanding mechanisms underlying various diseases, including cancer and metabolic disorders. The study of CREBL2 recombinant proteins has enabled researchers to elucidate its functional properties and interactions at a molecular level. By expressing CREBL2 in a recombinant form, scientists can analyze its binding affinity to specific DNA sequences, characterize its post-translational modifications, and investigate its role in signaling pathways. Furthermore, understanding the structure-function relationship of CREBL2 through these recombinant studies provides insights into its regulatory mechanisms. As a result, the research surrounding CREBL2 recombinant proteins not only enhances our comprehension of the protein itself but also contributes to the broader understanding of cAMP signaling and its implications in health and disease.











