Analytical Data
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Gene name
EE
- Application
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Alternative Names
EE；HSCO；Persulfide dioxygenase ETHE1. mitochondrial
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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
O95571
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Expression Region
8-254aa
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AA Sequence
VARRQLSQRGGSGAPILLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA
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Molecular Weight
43.1 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
The study of Epsilon (EE) recombinant proteins has gained significant attention in recent years due to their versatile applications in biotechnology and medicine. Epsilon proteins are a class of proteins that can be engineered through recombinant DNA technology, allowing for the production of proteins with specific characteristics and functionalities. The background of this research is rooted in the need for high-purity proteins for various applications, such as enzyme production, vaccine development, and therapeutic protein formulation. As traditional methods of protein extraction from natural sources often yield low quantities and impure products, the use of recombinant DNA technology offers a more efficient and controlled approach to protein production. Additionally, Epsilon recombinant proteins have shown potential in research areas, including structural biology and molecular diagnostics, as they can be tailored to interact with specific biological targets. The growing interest in personalized medicine and targeted therapies further drives the research in this field, as engineered proteins may lead to the development of innovative treatments for diseases. Furthermore, advancements in expression systems, such as yeast, bacteria, and mammalian cells, have enhanced the efficiency and scalability of producing Epsilon recombinant proteins, paving the way for their application in clinical settings. Overall, the exploration of Epsilon recombinant proteins represents a promising frontier in protein engineering and its associated fields, with the potential to revolutionize therapeutic strategies and improve healthcare outcomes.
