Analytical Data
-
Gene name
serB
- Application
-
Alternative Names
O-phosphoserine phosphohydrolase
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0AGB0
-
Expression Region
1-322aa
-
Molecular Weight
51 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
SerB protein, known for its role in the biosynthesis of the amino acid L-serine, has garnered significant attention in various fields, including microbiology, biochemistry, and potential therapeutic applications. This enzyme, also referred to as phosphoglycerate dehydrogenase, catalyzes the conversion of 3-phosphoglycerate to L-serine, a crucial compound involved in protein synthesis, neurotransmitter production, and one-carbon metabolism. The exploration of SerB has implications not only for understanding metabolic pathways in microorganisms but also for biotechnology applications where L-serine can be instrumental in the production of pharmaceuticals and nutritional supplements. Additionally, the investigation of recombinant SerB proteins allows researchers to probe its structural and functional attributes, ultimately facilitating the development of efficient biocatalysts. Given the rising interest in amino acid production and the need for sustainable bioprocesses, the recombinant expression of SerB in model organisms can provide insights into its enzymatic mechanism and regulation. Understanding SerB's function and properties opens new avenues for interventions in metabolic disorders and enhances our ability to engineer microbial strains for better amino acid production, positioning SerB as a key focus in metabolic engineering and synthetic biology studies.
