Analytical Data
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Gene name
DUSP12
- Application
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Alternative Names
Dual specificity phosphatase 12; Dual specificity protein phosphatase 12; Dual specificity tyrosine phosphatase YVH1; DUS12_HUMAN; DUSP 1; DUSP 12; DUSP1; DUSP12; Serine/threonine specific protein phosphatase; TDSP4; YVH 1; YVH1
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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
Q9UNI6
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Expression Region
1-340aa
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AA Sequence
MLEAPGPSDGCELSNPSASRVSCAGQMLEVQPGLYFGGAAAVAEPDHLREAGITAVLTVDSEEPSFKAGPGVEDLWRLFVPALDKPETDLLSHLDRCVAFIGQARAEGRAVLVHCHAGVSRSVAIITAFLMKTDQLPFEKAYEKLQILKPEAKMNEGFEWQLKLYQAMGYEVDTSSAIYKQYRLQKVTEKYPELQNLPQELFAVDPTTVSQGLKDEVLYKCRKCRRSLFRSSSILDHREGSGPIAFAHKRMTPSSMLTTGRQAQCTSYFIEPVQWMESALLGVMDGQLLCPKCSAKLGSFNWYGEQCSCGRWITPAFQIHKNRVDEMKILPVLGSQTGKI
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Molecular Weight
63.03 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
DUSP12 (Dual Specificity Phosphatase 12) is a member of the dual specificity phosphatase family, which plays a critical role in regulating various cellular processes, including cell proliferation, differentiation, and apoptosis by dephosphorylating both tyrosine and serine/threonine residues in target proteins. Research has shown that DUSP12 is involved in the negative regulation of the MAPK signaling pathways, which are crucial for cellular response to various stimuli. Its expression has been linked to several physiological and pathological conditions, including cancer and autoimmune diseases. Understanding the function of DUSP12 is important because it may provide insights into the mechanisms underlying these diseases and identify potential therapeutic targets. The production of recombinant DUSP12 protein allows for detailed in vitro studies of its biochemical properties and interactions with other signaling molecules, facilitating the exploration of its role in different cellular contexts. Additionally, the purification and characterization of the recombinant protein can aid in the development of specific inhibitors, which could have therapeutic implications. Increased interest in DUSP12 research stems from its potential as a biomarker for disease progression and as a target for innovative drug development strategies. Thus, the study of DUSP12 and its recombinant protein is a promising area of research in the field of molecular biology and biomedical science, with significant implications for understanding and treating various diseases.
