Analytical Data
-
Gene name
eta
- Application
-
Alternative Names
eta；Diacylglycerol kinase eta
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P11439
-
Expression Region
413-638aa
-
AA Sequence
ALLERNYPTGAEFLGDGGDISFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTGLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPREDLK
-
Molecular Weight
39.9 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
Research on Eta-like recombinant proteins has gained traction due to their potential applications in biotechnology and medicine. Eta proteins, which are characterized by their unique structural features and functionalities, play a crucial role in various biological processes. Their recombinant forms can be produced using techniques such as recombinant DNA technology, allowing for large-scale production and easier manipulation for experimental purposes. These proteins have shown promise in enzyme engineering, vaccine development, and as therapeutic agents in treating diseases. Moreover, studies have demonstrated that Eta proteins possess specific interaction capabilities, which can be harnessed for targeted drug delivery systems and biomolecular sensors. The increased interest in Eta proteins also stems from the need for sustainable bioprocessing in industrial applications, where engineered proteins can improve efficiency and reduce environmental impact. Ongoing research aims to further elucidate the molecular mechanisms underlying the functionality of these proteins, as well as to explore their possible modifications to enhance their properties for specific applications. As the field advances, Eta-like recombinant proteins are anticipated to contribute significantly to innovations in health care and environmental sustainability, demonstrating their importance in contemporary scientific research.
