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Mouse Anti-BCHE Recombinant Antibody (CBYY-0295) (CBMAB-0296-YY)

This product is mouse antibody that recognizes BCHE. The antibody CBYY-0295 can be used for immunoassay techniques such as: FC, WB
See all BCHE antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-0295
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Full length human recombinant protein of human BCHE produced in HEK293T cell.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:2,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
C-terminus

Target

Full Name
Butyrylcholinesterase
Introduction
This gene encodes a cholinesterase enzyme and member of the type-B carBovinexylesterase/lipase family of proteins. The encoded enzyme exhibits broad substrate specificity and is involved in the detoxification of poisons including organophosphate nerve agents and pesticides, and the metaBovinelism of drugs including cocaine, heroin and aspirin. Humans homozygous for certain mutations in this gene exhibit prolonged apnea after administration of the muscle relaxant succinylcholine.
Entrez Gene ID
Human590
Dog488143
UniProt ID
HumanP06276
DogP32750
Alternative Names
Butyrylcholinesterase; Acylcholine Acylhydrolase; Cholinesterase (Serum) 2; Butyrylcholine Esterase; Pseudocholinesterase; Choline Esterase II; Cholinesterase 1;
Function
Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Biological Process
Choline metabolic process Source: Ensembl
Cocaine metabolic process Source: UniProtKB
Learning Source: Ensembl
Negative regulation of cell population proliferation Source: Ensembl
Negative regulation of synaptic transmission Source: Ensembl
Neuroblast differentiation Source: Ensembl
Response to alkaloid Source: Ensembl
Response to drug Source: Ensembl
Response to folic acid Source: Ensembl
Response to glucocorticoid Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Butyrylcholinesterase deficiency (BCHED): An autosomal recessive metabolic condition characterized by increased sensitivity to certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium. BCHED results in slower hydrolysis of these drugs and, consequently, a prolonged neuromuscular block, leading to apnea. The duration of the prolonged apnea varies significantly depending on the extent of the enzyme deficiency.
PTM
N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type.

Xing, S., Li, Q., Xiong, B., Chen, Y., Feng, F., Liu, W., & Sun, H. (2021). Structure and therapeutic uses of butyrylcholinesterase: Application in detoxification, Alzheimer's disease, and fat metabolism. Medicinal Research Reviews, 41(2), 858-901.

Li, Q., Chen, Y., Xing, S., Liao, Q., Xiong, B., Wang, Y., ... & Sun, H. (2021). Highly Potent and Selective Butyrylcholinesterase Inhibitors for Cognitive Improvement and Neuroprotection. Journal of Medicinal Chemistry.

Pohanka, M., & Zakova, J. (2021). A Smartphone Camera Colorimetric Assay of Acetylcholinesterase and Butyrylcholinesterase Activity. Sensors, 21(5), 1796.

Jasiecki, J., & Wasąg, B. (2019). Butyrylcholinesterase protein ends in the pathogenesis of alzheimer’s disease—could BCHE genotyping Be helpful in Alzheimer’s therapy?. Biomolecules, 9(10), 592.

Zorbaz, T., Malinak, D., Kuca, K., Musilek, K., & Kovarik, Z. (2019). Butyrylcholinesterase inhibited by nerve agents is efficiently reactivated with chlorinated pyridinium oximes. Chemico-biological interactions, 307, 16-20.

Boyko, K. M., Baymukhametov, T. N., Chesnokov, Y. M., Hons, M., Lushchekina, S. V., Konarev, P. V., ... & Kovalchuk, M. V. (2019). 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD. Biochimie, 156, 196-205.

Lu, X., Yang, H., Li, Q., Chen, Y., Li, Q., Zhou, Y., ... & Sun, H. (2019). Expansion of the scaffold diversity for the development of highly selective butyrylcholinesterase (BChE) inhibitors: Discovery of new hits through the pharmacophore model generation, virtual screening and molecular dynamics simulation. Bioorganic chemistry, 85, 117-127.

Liu, S. Y., Xiong, H., Yang, J. Q., Yang, S. H., Li, Y., Yang, W. C., & Yang, G. F. (2018). Discovery of butyrylcholinesterase-activated near-infrared fluorogenic probe for live-cell and in vivo imaging. ACS sensors, 3(10), 2118-2128.

Dong, M. X., Xu, X. M., Hu, L., Liu, Y., Huang, Y. J., & Wei, Y. D. (2017). Serum butyrylcholinesterase activity: a biomarker for Parkinson’s disease and related dementia. BioMed research international, 2017.

Onder, S., David, E., Tacal, O., Schopfer, L. M., & Lockridge, O. (2017). Hupresin retains binding capacity for butyrylcholinesterase and acetylcholinesterase after sanitation with sodium hydroxide. Frontiers in pharmacology, 8, 713.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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