The alteration of BCHE expression activity caused by gene mutation is closely related to the pathogenesis of various academic diagnosis research and individual differences in drug response. Creative Biolabs has focused on establishing a one-stop solution for BCHE analysis, based on the wealth of data generated from our global footprint and understanding of its structure and function.
Human BCHE monomer contains 602 amino acids, and organophosphorus compounds can irreversibly inhibit the activity of BCHE. BCHE is known to exist as monomer, dimer, and tetramer, and the half-life of circulating BCHE depends on the tetramer form of the protein.
BCHE tetramer are four identical subunits of 85 kDa forming a tetramer that interacts via a C-terminal quadruple helix beam. The natural plasma BCHE tetramer is associated with a different fragment of a PRAD2-containing peptide, and the association of this peptide with a proline-rich peptide results in the stability of the BCHE tetramer in the blood.
Fig.1 The structure of BCHE.1
Studies on BCHE mainly focus on hereditary BCHE deficiency (mutation of BCHE gene located in chromosome 3,3 q26.1-q26.2) and BCHE-K variation. Other mutations also have a lot of pharmacological and clinical significance in recent years, is also growing interest in the development of BCHE inhibitors. Recent studies on BCHE are as follows:
The pathogenesis is thought to be related to BCHE mutation and BCHE polymorphism. BCHE is considered as a new target for the treatment of AD, and tryptophan-derived butyryl cholinesterase inhibitors are expected to be its lead agents.
Many studies have found that the activity of BCHE and its gene polymorphism are related to the metabolic characteristics of obesity. BCHE activity has been shown to be positively correlated with body mass and body mass index (BMI).
Babies with lower BCHE levels had a much higher risk of dying from SIDS. BCHE plays an important function in the brain's arousal pathways, and its deficiency is likely an indication of insufficient arousal, which reduces infants' ability to wake up or respond to external environments, making them susceptible to SIDS.
Patients who develop sustained nerve muscle block (NMB) after anesthesia succinylcholine use usually carry a BCHE variant, reduced enzyme activity, or acquired BCHE deficiency. Hereditary BCHE defects are caused by mutations in the BCHE gene located on chromosome 3,3 q26.1-q26.2.
BCHE can be used as a stoichiometric biological scrubber for organophosphorus pesticides and nerve agents, thereby protecting acetylcholinesterase from irreversible inhibition of these substances.
BCHE mutants are expected to be used as target drugs for cocaine abuse by changing the short half-life of BCHE with gene editing technology.
BCHE variation and BCHE polymorphism are related to the pathogenesis of a variety of diseases, with the continuous improvement of medical technology and the continuous investment of basic research, BCHE related biomarkers can be widely applied. Our services can be customized to suit the specific needs of our clients, popular analysis services targeting BCHE include but are not limited to the following:
| Cat | Service |
|---|---|
| BAS109-1 | BCHE Antibody Development |
| BAS109-2 | BCHE Protein Expression |
| BAS109-3 | BCHE Mutants Expression |
| BAS109-4 | BCHE Gene Analysis |
| BAS109-5 | BCHE ELISA Assay |
| Cat | Service |
|---|---|
| BAS109-6 | BCHE Inhibitor Screening Assay |
| BAS109-7 | BCHE Inhibitory Activity Assay |
| BAS109-8 | BCHE Enzyme Assay |
| BAS109-9 | BCHE Chemistry Analysis |
Creative Biolabs is committed to providing the highest quality of custom services and products at the most reasonable prices. Please feel free to contact us for more information and a formal quote.
Reference
For Research Use Only.