Analytical Data
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Gene name
SPRED2
- Application
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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
Q7Z698
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Expression Region
Met1~Ala418
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Molecular Weight
51kDa
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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
SPRED2, or Sprouty-related EVH1 domain-containing protein 2, is a vital signaling molecule involved in the regulation of various cellular processes, including cell proliferation, differentiation, and migration. It acts primarily as a negative regulator of the MAPK/ERK signaling pathways, which are crucial for transmitting extracellular signals to the nucleus, thereby influencing a myriad of biological functions. Dysregulation of SPRED2 has been implicated in several diseases, including cancer and developmental disorders, highlighting its potential as a therapeutic target. The study of SPRED2 recombinant proteins has garnered attention as researchers aim to elucidate the mechanistic details of its function and interaction with other signaling molecules. Recombinant SPRED2 can be produced in various expression systems, allowing for detailed investigations of its biochemical properties, structural characteristics, and binding affinities. Understanding SPRED2’s role at the molecular level may lead to the identification of novel intervention strategies to manipulate its activity in pathological conditions. Furthermore, the study of SPRED2 is important as it contributes to the broader field of signal transduction and its implications in health and disease. Therefore, the production and analysis of SPRED2 recombinant proteins are crucial for advancing our understanding of its biology and exploring its potential in biomedical applications.
