BCHE(1E8) Antibody (YA7325)
(Synonyms: Cholinesterase, Acylcholine acylhydrolase, Butyrylcholine esterase, Choline esterase II, Pseudocholinesterase, Bche)BCHE(1E8) Antibody (YA7325) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to BCHE(1E8).
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Host:
Mouse
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Isotype:
IgG
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Application:
IHC-P, IHC-F, IF-Tissue
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Reactivity :
Rat
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Formulation:
Supplied in 0.01M tris buffered saline (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
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Conjugation:
Non-conjugated
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IHC-F
IHC-F: Immunohistochemistry-Frozen
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IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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|---|---|---|---|
| Dilution Ratio | 1:100-500 | 1:100-500 | 1:100-500 |
Product Details
BCHE(1E8) Antibody (YA7325) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to BCHE(1E8).
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Host Mouse
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Clonality Monoclonal
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Species ReactivityRat Predicted Reactivity: HumanNote: The predicted reactivity is for reference only and should not be considered a guarantee of product performance.
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Calculated Molecular Weight Predicted band size: 66 kDa;
Human BCHE native protein purified
Endogenous
affinity purified by Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 0.01M tris buffered saline (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Butyrylcholinesterase (BChE, EC 3.1.1.8) is a cholinesterase family enzyme that hydrolyzes a broad range of choline esters and other ester-containing substrates, contributing to cholinergic regulation as well as xenobiotic detoxification processes[1][2]. BChE is widely distributed in human tissues and plasma, where it participates in cholinergic transmission, ester metabolism, and the neutralization of toxic compounds including organophosphates and carbamates[1]. Mechanistically, BChE functions as a hydrolytic enzyme that can buffer acetylcholine metabolism when acetylcholinesterase (AChE) activity is reduced, thereby influencing cholinergic homeostasis[2]. In disease contexts, increasing evidence links BChE to neurodegenerative disorders, particularly Alzheimer’s disease (AD), where BChE activity and expression become more prominent during disease progression and are associated with late-stage cholinergic dysfunction[3][4]. Experimental studies therefore consider BChE an important therapeutic target and biomarker candidate for AD-related research[3][4]. Compared with the closely related isoform AChE, which primarily terminates synaptic acetylcholine signaling, BChE exhibits broader substrate specificity, distinct tissue distribution, and a stronger role in drug metabolism, detoxification, and non-neuronal physiological processes[1][2]. For experimental applications, selective BChE inhibitors are widely used to investigate cholinergic mechanisms and have been developed as pharmacological tools for evaluating therapeutic strategies in neurodegenerative disease models, with high selectivity over AChE considered a key design objective[3][4].
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Subcellular Localization
Secreted
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Expression
Tissue_Specificity: Detected in blood plasma (at protein level). Present in most cells except erythrocytes -
Isoforms & Post-Translational Modification
P06276: 602 amino acids, molecular weight 68418 Da.
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Subunit
Homotetramer; disulfide-linked
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SwissProt ID
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Synonyms
Cholinesterase, Acylcholine acylhydrolase, Butyrylcholine esterase, Choline esterase II, Pseudocholinesterase, Bche
Documentation
[1]. Hajimohammadi S, et al. New views on physiological functions and regulation of butyrylcholinesterase and potential therapeutic interventions. Front Mol Biosci. 2025 Jun 19;12:1625318. [Content Brief]
[2]. Jovičić SM. Enzyme ChE, et al. Enzyme ChE, cholinergic therapy and molecular docking: Significant considerations and future perspectives. Int J Immunopathol Pharmacol. 2024 Jan-Dec;38:3946320241289013. [Content Brief]
[3]. Brus B, et al. Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor. J Med Chem. 2014 Oct 9;57(19):8167-79. [Content Brief]
[4]. Zhou Y, et al. Discovery of Selective Butyrylcholinesterase (BChE) Inhibitors through a Combination of Computational Studies and Biological Evaluations. Molecules. 2019 Nov 20;24(23):4217. [Content Brief]