Analytical Data
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Gene name
DUSP6
- Application
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Alternative Names
DUSP6；MKP3；PYST1;Dual specificity Protein phosphatase 6
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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
Q16828
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Expression Region
1-381aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MIDTLRPVPF ASEMAISKTV AWLNEQLELG NERLLLMDCR PQELYESSHI ESAINVAIPG IMLRRLQKGN LPVRALFTRG EDRDRFTRRC GTDTVVLYDE SSSDWNENTG GESVLGLLLK KLKDEGCRAF YLEGGFSKFQ AEFSLHCETN LDGSCSSSSP PLPVLGLGGL RISSDSSSDI ESDLDRDPNS ATDSDGSPLS NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT PNLPNLFENA GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS SPCDNRVPAQ QLYFTTPSNQ NVYQVDSLQS T
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Molecular Weight
44 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
DUSP6, or Dual Specificity Phosphatase 6, is a member of the dual specificity phosphatase family, which plays a pivotal role in the regulation of MAPK (Mitogen-Activated Protein Kinase) signaling pathways. The dysregulation of DUSP6 has been implicated in various pathological conditions, including cancer, cardiovascular diseases, and developmental disorders. Unlike many phosphatases that are specific for either serine-threonine or tyrosine residues, DUSP6 can dephosphorylate both types, adding complexity to its regulatory functions in cellular signaling. Research has shown that DUSP6 acts as a negative regulator of ERK (Extracellular Signal-Regulated Kinase) signaling by dephosphorylating ERK1 and ERK2, thereby modulating cell proliferation, differentiation, and survival. Its specific expression patterns during development and in various tissues highlight its potential as a biomarker and therapeutic target. Understanding the structure and function of DUSP6 through studies involving recombinant protein technology can provide insights into its biological roles and regulatory mechanisms. Such research has the potential to inform the design of DUSP6-targeted therapies, enhancing therapeutic strategies for diseases where DUSP6 is a contributing factor. Thus, the investigation of DUSP6 recombinant proteins not only advances fundamental biochemical knowledge but also opens avenues for translational applications in medicine.
