BCHE antibody from Promab.
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Esterase with broad substrate specificity. BCHE contributes to the inactivation of the neurotransmitter acetylcholine. BCHE can degrade neurotoxic organophosphate esters.
For research use only.
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species | WB | IHC | IHC-P | IHC-F | IF/ICC | Flow Cytometry | ELISA | IP | ChIP |
|---|---|---|---|---|---|---|---|---|---|
| Human | |||||||||
| Mouse |
This product is manufactured by Promab and sold through ABMIUM without relabelling.
ABMIUM supports global orders. Availability, shipping requirements and applicable import arrangements are confirmed before fulfilment where required.
Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
Butyrylcholinesterase (BCHE) is a secreted cholinesterase with broad ester-hydrolysing activity. It is studied alongside acetylcholinesterase in cholinergic enzymology and in work examining ester metabolism, enzyme activity and BCHE genetic variation.
Biological function: BCHE is a serine hydrolase that hydrolyses choline esters and other ester-containing substrates. Compared with acetylcholinesterase, butyrylcholinesterase has broader substrate specificity and contributes substantially to plasma cholinesterase activity and metabolism of multiple ester substrates.
