Analytical Data
-
Gene name
D13
- Application
-
Alternative Names
D13
-
Species
Virus
-
Source
E. coli
-
Tag
Strep;His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
YP_010377107.1
-
Expression Region
M1-N551
-
Protein Length
Full Length
-
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
The study of D13 recombinant protein has emerged as a significant area of interest within the field of molecular biology and protein engineering, particularly due to its potential applications in therapeutic and diagnostic contexts. D13 protein, a variant derived from a specific pathogen or mammalian source, has been shown to possess unique structural and functional characteristics that make it a promising candidate for various biomedical applications. Researchers are investigating the protein's role in immune response modulation, pathogen inhibition, and as a potential vaccine component. The development of recombinant D13 protein involves advanced genetic engineering techniques, allowing for the production of this protein in host organisms such as bacteria or yeast, which simplifies its purification and increases yield. Moreover, studies have demonstrated that modifications to the D13 protein can enhance its stability and activity, further broadening its applicability. The scientific community is keenly focused on elucidating the molecular mechanisms behind D13’s functions and interactions, aiming to harness these properties for innovative healthcare solutions. As a result, D13 recombinant protein research has the potential to contribute significantly to advancements in immunotherapy, vaccine development, and the creation of novel diagnostic tools, ultimately improving health outcomes in various disease contexts.
