SAB4200839

Sigma-Aldrich

Anti-Acetylcholinesterase (AChE) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):
AChE
Pricing and availability is not currently available.

biological source

rabbit

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

application(s)

immunoblotting: 1:1000-1:2000 using whole extracts of Jurkat cells.
immunofluorescence: 1:1000-1:20000 using Human A431

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... ACHE(43)

Related Categories

General description

Acetylcholinesterase (AChE) is a member of the a/ß-hydrolase-fold proteins superfamily which is composed of structurally related proteins with a great diversity in their catalytic, recognition, adhesion and chaperone functions. 3D structure studies of a/ß-hydrolase reviled a variety of folding patterns suggesting associations through oligomerization dependent functions.1 AChE is a tissue specific serine hydrolase expressed in several variants at neuromuscular junctions (NMJs)2, cholinergic brain synapses2-3 or erythrocyte (Red Blood Cells- RBC)4.

Specificity

Anti-Acetylcholinesterase (AChE) antibody specifically recognizes human AChE.

Immunogen

human Acetylcholinesterase, recombinant, expressed in HEK 293 cells

Application

The antibody may be used in various immunochemical techniques including Immunoblotting Immunofluorescence and ELISA. Detection of the AChE band by Immunoblotting is specifically inhibited by the immunogen.

Biochem/physiol Actions

In the synaptic cleft, AChE main function is to ensure rapid hydrolysis of acetylcholine (ACh) released from motor nerve ending into choline and acetic acid thus preventing postsynaptic muscle ACh receptors (AChR) hyperactivation and termination of the signal transmission.2-3,5AChE and Butyrylcholinesterase (BChE) inhibitory drugs or peptides are being used in several neurodegenerative diseases including Alzheimer′s disease and pathological muscle weakness such as Myasthenia Gravis. These AChE inhibitors increase synaptic ACh levels and hence improve the cholinergic function in the brain.2-3,5-6 Erythrocytes AChE (AChE-H) is a membrane encored AChE splicing variant found in RBC, it belongs to the glycosylphosphatidylinositol (GPI) protein family and carries the Yta blood group antigen. Erythrocytes AChE can be found in plasma circulating vesicles originated from aged erythrocytes, and therefore is considered as a biomarker for RBC membrane integrity. Furthermore, Erythrocytes AChE activity is also a marker for inflammation and other diseases including essential hypertension, glaucoma, ALS, neurotoxicity, and Hirschsprung′s disease.4,7-8

Physical form

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

Storage and Stability

For continuous use, store at 2-8°C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Antonella De Jaco et al.
The FEBS journal, 279(23), 4293-4305 (2012-10-06)
The α/β-hydrolase fold superfamily of proteins is composed of structurally related members that, despite great diversity in their catalytic, recognition, adhesion and chaperone functions, share a common fold governed by homologous residues and conserved disulfide bridges. Non-synonymous single nucleotide polymorphisms...
Vivek Kumar Gupta et al.
Enzyme research, 2015, 370705-370705 (2015-11-26)
Lead induced neurotoxicity in the people engaged in different occupations has received wide attention but very little studies have been carried out to monitor occupational neurotoxicity directly due to lead exposure using biochemical methods. In the present paper an endeavour...
Thaiane Coelho Dos Santos et al.
Frontiers in pharmacology, 9, 1192-1192 (2018-11-09)
Alzheimer's disease (AD) is a main cause of dementia, accounting for up to 75% of all dementia cases. Pathophysiological processes described for AD progression involve neurons and synapses degeneration, mainly characterized by cholinergic impairment. This feature makes acetylcholinesterase inhibitors (AChEi)...
Aiqiong Chen et al.
Environmental science & technology, 46(3), 1828-1833 (2012-01-03)
Acetylcholinesterase (AChE) enzyme activity in red blood cells (RBCs) is a useful biomarker for biomonitoring of exposures to organophosphorus (OP) pesticides and chemical nerve agents. In this paper, we reported a new method for AChE activity assay based on selective...
Vivitri Prasasty et al.
Molecules (Basel, Switzerland), 23(9) (2018-09-16)
Acetylcholinesterase-inhibitory peptide has gained much importance since it can inhibit acetylcholinesterase (AChE) and increase the availability of acetylcholine in cholinergic synapses, enhancing cholinergic transmission in pharmacological treatment of Alzheimer's disease (AD). Natural peptides have received considerable attention as biologically important...

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.