Analytical Data
-
Gene name
Butyrylcholinesterase/BCHE
- Application
-
Alternative Names
BuChE; CHE1; E1; Pseudocholinesterase; Cholinesterase; Acylcholine acylhydrolase; Butyrylcholine esterase; Choline esterase II
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P06276
-
Expression Region
Val420~Leu602
-
Molecular Weight
26kDa
-
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
Butyrylcholinesterase (BCHE) is a crucial enzyme involved in the hydrolysis of acetylcholine and various other ester-containing compounds, playing a vital role in the regulation of neurotransmission and drug metabolism. The enzyme's significance extends to clinical applications, particularly in the detoxification of certain organophosphate compounds and as a biomarker for various neurological disorders. Recent research has increasingly focused on the production of recombinant BCHE to overcome limitations associated with native enzyme sources, such as low yield and stability issues. Recombinant BCHE offers several advantages, including improved enzymatic activity, enhanced stability under varying conditions, and the potential for large-scale production through biotechnological methods. Advances in genetic engineering and protein expression systems have facilitated the generation of recombinant BCHE with tailored properties suitable for industrial and therapeutic applications. Understanding the structure-function relationship of BCHE is also essential, as modifications can optimize its effectiveness in clinical scenarios, particularly in organophosphate poisoning treatment and as a potential therapeutic target in neurodegenerative diseases. Overall, the exploration of recombinant BCHE represents a significant step toward harnessing its potential in both research and clinical settings, providing a platform for further advancements in pharmacology and toxicology.
