Analytical Data
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Gene name
DUSP4
- Application
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Alternative Names
Homo sapiens (Human)
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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
Q13115
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Expression Region
1-394aa
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AA Sequence
MVTMEELREMDCSVLKRLMNRDENGGGAGGSGSHGTLGLPSGGKCLLLDCRPFLAHSAGYILGSVNVRCNTIVRRRAKGSVSLEQILPAEEEVRARLRSGLYSAVIVYDERSPRAESLREDSTVSLVVQALRRNAERTDICLLKGGYERFSSEYPEFCSKTKALAAIPPPVPPSATEPLDLGCSSCGTPLHDQGGPVEILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEYIDAVKDCRGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFESQVLATSCAAEAASPSGPLRERGKTPATPTSQFVFSFPVSVGVHSAPSSLPYLHSPITTSPSC
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Molecular Weight
49.9 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
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Protein Description
DUSP4, or Dual Specificity Phosphatase 4, is a member of the dual specificity phosphatase family, which plays a significant role in regulating cellular signaling pathways by dephosphorylating both tyrosine and serine/threonine residues. Research has highlighted that DUSP4 is implicated in various biological processes, including cell proliferation, differentiation, and apoptosis, making it a crucial player in maintaining cellular homeostasis. Dysregulation of DUSP4 has been linked to several pathological conditions, including cancer and inflammatory diseases, emphasizing the importance of understanding its function and regulation. The study of recombinant DUSP4 protein has garnered attention as it provides insights into the structure-function relationship of the phosphatase and its role in cellular signaling networks. By producing recombinant DUSP4, researchers can investigate its enzymatic activity, interaction with substrates and other signaling molecules, and its potential as a therapeutic target. Moreover, studying the recombinant form facilitates the exploration of post-translational modifications and the identification of small molecule inhibitors, thereby advancing our understanding of its contribution to disease mechanisms and therapeutic strategies. Overall, the exploration of DUSP4 and its recombinant protein forms holds significant promise for uncovering novel insights into cellular signaling and disease pathogenesis.
