Analytical Data
-
Gene name
DUSP13
- Application
-
Alternative Names
Branching-enzyme interacting DSPMuscle-restricted DSP ;MDSP
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6B8I1
-
Expression Region
1-198aa
-
Molecular Weight
36.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DUSP13, also known as dual specificity phosphatase 13, is a member of the dual specificity phosphatase family, which plays a crucial role in various cellular processes by dephosphorylating both tyrosine and serine/threonine residues. This protein has garnered attention due to its involvement in signaling pathways related to cell growth, differentiation, and apoptosis. Research has shown that DUSP13 is implicated in several diseases, including cancer and neurological disorders, suggesting its potential as a therapeutic target. The functional characterization of DUSP13 requires the generation of recombinant protein, which facilitates the study of its enzymatic activity, substrate specificity, and interaction with other signaling molecules. Moreover, understanding the regulation of DUSP13 activity could provide insights into its role in disease mechanisms and highlight its potential as a biomarker or drug target. Given the growing interest in the therapeutic implications of phosphatases, research on DUSP13 recombinant protein is vital for exploring its biological functions and developing novel strategies for treatment.
