Analytical Data
-
Gene name
treZ
-
简介
The treZ protein plays a key role in glycan biosynthesis, especially trehalose biosynthesis. This enzyme helps catalyze the formation of trehalose, a disaccharide made of two glucose molecules linked by an α,α-1,1-glycosidic bond. treZ Protein, Arthrobacter ramosus (FLAG, His) is the recombinant treZ protein, expressed by E. coli , with N-6*His, N-Flag labeled tag.
- Application
-
Alternative Names
treZ; Malto-oligosyltrehalose trehalohydrolase; MTHase; 4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase; Maltooligosyl trehalose trehalohydrolase
-
Species
Others
-
Source
E. coli
-
Tag
N-6*His;N-Flag
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9AJN6
-
Expression Region
M1-E575
-
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
TreZ, a member of the trehalose biosynthesis pathway, is a crucial enzyme in various microorganisms, including bacteria and fungi, where it catalyzes the conversion of trehalose to glucose. Trehalose serves as a vital metabolite that helps organisms survive under stress conditions, such as heat, desiccation, and oxidative stress. Recent studies have shown that trehalose can play a protective role in cellular processes, including protein folding and stabilization, which has generated interest in treZ as a potential target for biotechnological applications. The recombinant expression of treZ facilitates the production of trehalose in controlled environments, providing insights into its enzymatic functions and potential therapeutic benefits in stress resistance and metabolic regulation. Understanding the structural and functional properties of treZ can pave the way for advancements in genetic engineering, agriculture, and the development of novel stress-resistant crops. Furthermore, investigations into the treZ gene and its protein product enhance our comprehension of trehalose metabolism, leading to potential applications in human health, such as enhancing cellular tolerance to inhospitable conditions and improving the efficacy of certain pharmaceuticals. The ongoing research in treZ recombinant protein not only augments our biological knowledge but also has promising implications for industrial biotechnology and medical research.











