Analytical Data
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Gene name
PTPMT1
- Application
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Alternative Names
PTEN-like phosphatasePhosphoinositide lipid phosphataseProtein-tyrosine phosphatase mitochondrial 1 (EC:3.1.3.16, EC:3.1.3.48)
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WUK0
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Expression Region
28-201aa
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Molecular Weight
35.9 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
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Protein Description
PTPMT1 (Protein Tyrosine Phosphatase Methylesterase 1) is an important enzyme involved in various cellular processes, including signaling pathways related to cell growth, differentiation, and metabolism. Its role in the regulation of protein tyrosine phosphorylation makes it a significant target for understanding the intricacies of cellular signaling networks. The aberrant expression or dysfunction of PTPMT1 has been implicated in several diseases, including cancer and metabolic disorders, highlighting its potential as a biomarker and therapeutic target. Research into the recombinant expression of PTPMT1 aids in the elucidation of its structure-function relationship and facilitates the development of inhibitors that can modulate its activity. Recombinant proteins allow for detailed studies of enzymatic mechanisms and interactions with other cellular components, providing insights that may lead to novel therapeutic strategies. Additionally, understanding the regulation of PTPMT1 can pave the way for interventions aimed at restoring normal cellular function in disease states. As a result, the study of PTPMT1 is crucial not only for basic biomedical research but also for the development of targeted therapies in clinical settings.
