Analytical Data
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Gene name
DUSP23
- Application
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Alternative Names
DUSP23；LDP3；VHZ;Dual specificity Protein phosphatase 23
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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
Q9BVJ7
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Expression Region
1-150aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGVQPPNFSWVLPGRLAGLALPRLPAHYQF LLDLGVRHLVSLTERGPPHSDSCPGLTLHRLRIPDFCPPAPDQIDRFVQI VDEANARGEAVGVHCALGFGRTGTMLACYLVKERGLAAGDAIAEIRRLRP GSIETYEQEKAVFQFYQRTK
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Molecular Weight
19 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
DUSP23, a member of the dual-specificity phosphatase (DUSP) family, plays a significant role in regulating cellular signaling pathways by dephosphorylating both tyrosine and serine/threonine residues on target proteins. This phosphatase is implicated in various physiological processes, including cell proliferation, differentiation, and stress responses. Alterations in DUSP23 expression have been linked to several diseases, including cancer and neurodegenerative disorders, making it a potential therapeutic target. The study of DUSP23 recombinant protein aims to elucidate its biochemical properties and cellular functions, providing insights into its role in various signaling cascades. By generating and characterizing DUSP23 recombinant protein, researchers can explore its interactions with specific substrates, identify regulatory mechanisms, and investigate its impact on downstream signaling pathways. Understanding the structure-function relationship of DUSP23 can also contribute to the development of novel therapeutic approaches aimed at modulating its activity in disease contexts. Overall, research on DUSP23 recombinant protein holds promise for advancing our understanding of phosphatase biology and its implications in health and disease.
