Analytical Data
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Gene name
SPRY4
- 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
Q9C004
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Expression Region
Met1~Phe299
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Molecular Weight
38kDa
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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
SPRY4 (Sprouty homolog 4) is an important protein implicated in various cellular processes, including growth factor signaling, cell proliferation, and differentiation. It belongs to the Sprouty family of proteins, which act as negative regulators of receptor tyrosine kinase pathways, particularly the Epidermal Growth Factor (EGF) and Fibroblast Growth Factor (FGF) signaling. Dysregulation of SPRY4 has been linked to several diseases, including cancer, where it may function as a tumor suppressor or an oncogene depending on the context. Research on SPRY4 has gained momentum due to its potential therapeutic implications; understanding its structure and function could unveil new strategies for targeted therapies. The production and characterization of SPRY4 recombinant protein are crucial for studying its biochemical properties and interactions with other signaling molecules. Additionally, investigating the role of SPRY4 in specific cellular contexts could provide insights into its mechanisms in development and disease progression. Thus, the reconstitution of SPRY4 through recombinant techniques serves as a foundational step in elucidating its biological roles and exploring its potential as a drug target in cancer and other pathologies.
