Analytical Data
-
Gene name
SH-1
- Application
-
Alternative Names
Shrunken-1 Sucrose-UDP glucosyltransferase 1
-
Species
Zea mays
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P04712
-
Expression Region
555-802aa
-
Molecular Weight
44.8 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
SH-1 recombinant protein is derived from the SH-1 protein, which is known for its role in various biological processes, including immune response regulation and cell signaling. Research into SH-1 has gained significant attention due to its potential applications in therapeutic interventions and vaccine development. The protein has been implicated in modulating immune responses, making it a candidate for enhancing vaccine efficacy against infectious diseases and possibly cancer. The understanding of SH-1's structure and function has been deepened through recombinant DNA technology, allowing for the production of the protein in sufficient quantities for detailed study. Investigations into its properties, interactions with other biomolecules, and mechanisms of action are crucial for developing targeted therapies. Additionally, the recombinant nature of SH-1 enables researchers to engineer variants for optimized performance, further enhancing its utility in clinical applications. As such, the study of SH-1 recombinant protein is not only important for basic biological research but also for advancing potential medical innovations.
