Analytical Data
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Gene name
AMSH
- Application
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Alternative Names
AMSH; Associated molecule with the SH3 domain of STAM; Endosome-associated ubiquitin isopeptidase
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9CQ26
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Expression Region
Glu166~Cys406
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Molecular Weight
27kDa
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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
AMSH (Associated Molecule with the SH3 Domain of STAM) is a deubiquitinating enzyme that plays a crucial role in various cellular processes, including the regulation of protein degradation, endosomal function, and intracellular signaling pathways. The significance of AMSH in the ubiquitin-proteasome system (UPS) has attracted considerable interest among researchers, as it modulates the fate of ubiquitinated proteins by removing ubiquitin chains, thereby influencing protein stability and activity. Dysregulation of AMSH has been associated with several diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Investigating the structure and function of recombinant AMSH provides insights into its enzymatic mechanisms and interactions with substrate proteins, as well as its role in cellular homeostasis. Additionally, the ability to produce recombinant AMSH in a controlled environment facilitates studies on its kinetics, substrate specificity, and regulatory mechanisms, paving the way for the development of inhibitors that could serve as valuable tools in drug discovery and the treatment of AMSH-related diseases. Understanding AMSH's biological roles and regulatory pathways not only enhances our comprehension of the UPS but also opens avenues for innovative therapeutic strategies that target ubiquitin-related processes at large. This research background underscores the importance of AMSH in cellular regulation and its potential implications in human health.
