Analytical Data
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Gene name
DUSP11
- Application
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Alternative Names
DUSP11; PIR1RNA/RNP complex-1-interacting phosphatase; EC 3.1.3.-; Dual specificity protein phosphatase 11; Phosphatase that interacts with RNA/RNP complex 1
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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
O75319
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Expression Region
1-330aa
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AA Sequence
MSQWHHPRSGWGRRRDFSGRSSAKKKGGNHIPERWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLKIFTVGHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIRKNWNSSVPRSSDFEDSAHLMQPVHNKPVKQGPRYNLHQIQGHSAPRHFHTQTQSLQQSVRKFSENPHVYQRHHLPPPGPPGEDYSHRRYSWNVKPNASRAAQDRRRWYPYNYSRLSYPACWEWTQ
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Molecular Weight
65.3 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
DUSP11, a member of the dual-specificity phosphatase (DUSP) family, plays a crucial role in regulating various cellular signaling pathways by dephosphorylating both tyrosine and serine/threonine residues on target proteins. Understanding its biological functions is essential due to its involvement in important processes such as cell proliferation, differentiation, and apoptosis. Research on DUSP11 has gained traction in recent years, particularly concerning its implications in cancer biology and immune responses. Dysregulation of DUSP11 expression and activity has been linked to several diseases, including malignancies, highlighting its potential as a therapeutic target. Recombinant DUSP11 protein is utilized to investigate its enzymatic properties, substrate specificity, and interaction with other signaling molecules. These studies help elucidate the role of DUSP11 in pathological conditions and may pave the way for novel intervention strategies aimed at modulating its activity for clinical benefit. The generation of a recombinant form of DUSP11 allows for detailed biochemical assays and structural analyses, further contributing to our understanding of its function and regulation within the context of cellular signaling networks.











