Analytical Data
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Gene name
DUSP14
- Application
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Alternative Names
DUSP14；MKP6；Dual specificity Protein phosphatase 14
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95147
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Expression Region
1-198aa
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AA Sequence
MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI
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Molecular Weight
38.3kDa
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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
DUSP14, a member of the dual specificity phosphatase (DUSP) family, plays a critical role in cellular signaling by dephosphorylating both tyrosine and serine/threonine residues on its substrates, which include key mitogen-activated protein kinases (MAPKs). The dysregulation of DUSP14 has been implicated in various pathological conditions, including cancer, inflammatory diseases, and neurodegenerative disorders, making it a potential therapeutic target. Research on DUSP14 has gained momentum as scientists seek to elucidate its mechanisms of action in facilitating cellular responses to environmental stimuli. Understanding the structure and function of recombinant DUSP14 protein is essential for dissecting its role in cellular pathways and providing insights into its potential as a biomarker or therapeutic agent. Techniques such as protein expression in heterologous systems, characterization of enzymatic activity, and determination of substrate specificity are crucial for advancing our comprehension of DUSP14's biological functions. By creating recombinant versions of DUSP14, researchers can explore its interactions with MAPKs and other signaling molecules, paving the way for novel therapeutic strategies that leverage the modulation of DUSP14 activity in various diseases.
