Analytical Data
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Gene name
ECE2
- Application
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Alternative Names
Methyltransferase-like region
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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 90% as determined by SDS-PAGE.
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Uniprot
Q80Z60
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Expression Region
Met1~Phe163
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Molecular Weight
15&22kDa
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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
ECE2, or Endothelin-Converting Enzyme 2, is a pivotal enzyme involved in the enzymatic conversion of big endothelin-1 to its bioactive form, endothelin-1, which plays a crucial role in various physiological processes, including vascular homeostasis, blood pressure regulation, and cellular proliferation. Research on ECE2 has gained prominence due to its association with several cardiovascular diseases and pathological conditions, such as hypertension, heart failure, and pulmonary arterial hypertension. Understanding the structure and function of ECE2 is essential for developing targeted therapies aimed at modulating its activity. Recent advances in protein engineering and molecular biology have facilitated the expression and purification of recombinant ECE2, allowing for detailed studies on its catalytic mechanisms and interactions with substrates and inhibitors. These studies are crucial for identifying potential drug candidates and therapeutic approaches to mitigate the detrimental effects of excessive endothelin production. Furthermore, ECE2’s role in other biological pathways, such as inflammation and cancer, positions it as a significant research target for understanding complex disease mechanisms and developing novel therapeutic strategies. As the scientific community continues to uncover the multifaceted roles of ECE2, its potential as a biomarker and therapeutic target in various diseases remains an exciting area of exploration in biomedical research.
