Analytical Data
-
Gene name
Ba71V-107
- Application
-
Alternative Names
Ba71V-107; D117L; Major structural protein p17
-
Species
African swine fever virus
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q89424
-
Expression Region
1-117aa
-
Molecular Weight
19.2 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
The Ba71V-107 recombinant protein is derived from the Ba71V strain of the bovine viral diarrhea virus (BVDV), a member of the Flaviviridae family. BVDV poses significant threats to livestock health, leading to economic losses in the cattle industry due to decreased productivity and increased veterinary costs. The Ba71V-107 variant has been utilized in research as a model to study viral pathogenesis and immune response due to its well-characterized genetics and ability to induce a robust immune response in cattle. Understanding the structure and function of the Ba71V-107 recombinant protein can provide valuable insights into viral mechanisms, potential vaccine targets, and therapeutic interventions. Additionally, studying this protein can help decipher the host's immune response, which is crucial for developing effective vaccination strategies and improving herd immunity. Enhanced knowledge of Ba71V-107 and its interactions with host cells can facilitate the design of novel antiviral agents and contribute to the overall management of BVDV infections, ultimately benefiting livestock health and agricultural productivity. Ongoing research continues to explore the functional properties of Ba71V-107, aiming to unlock further potential for controlling this economically important viral infection in the cattle industry.











