Analytical Data
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Gene name
DUSP22
- Application
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Alternative Names
JNK-stimulatory phosphatase-1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NRW4
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Expression Region
1-184aa
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Molecular Weight
47.8 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
DUSP22 (Dual-specificity phosphatase 22) is a member of the dual-specificity phosphatase family, characterized by its ability to dephosphorylate both tyrosine and serine/threonine residues. This enzyme plays a critical role in regulating various cellular processes, including cell proliferation, differentiation, and apoptosis, by modulating signaling pathways such as the MAPK cascade. Abnormal expression or function of DUSP22 has been implicated in several diseases, including cancer and autoimmune disorders, which makes it a potential therapeutic target. Recent studies have highlighted the significance of DUSP22 in controlling immune responses, particularly in T-cells, by influencing the balance between activation and inhibition signals. To further explore its biological functions and therapeutic potential, researchers are focused on the production and characterization of recombinant DUSP22 proteins. This involves using recombinant DNA technology to express and purify DUSP22 in various systems, allowing for detailed biochemical assays and structural studies. Understanding DUSP22's mechanisms of action could lead to novel strategies for disease intervention, enhancing our ability to manipulate immune responses in clinical settings. Overall, the investigation of DUSP22 recombinant protein is essential for deciphering its role in cellular signaling and its implications in health and disease.
