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MAB5270

Sigma-Aldrich

Anti-Choline Acetyltransferase Antibody, clone 1.B3.9B3

clone 1.B3.9B3, Chemicon®, from mouse

Synonym(s):

ChAT

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

1.B3.9B3, monoclonal

species reactivity

human, rat, pig

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... CHAT(1103)
pig ... Chat(396896)
rat ... Chat(290567)

Specificity

Reacts with choline acetyltransferase (ChAT)-positive cells from humans, rats and pigs (Ostermann-Fatif et al., 1992a,b).

Immunogen

Highly purified ChAT obtained from porcine brain (Ostermann-Fatif et al., 1990).

Application

Research Category
Neuroscience
Research Sub Category
Neurotransmitters & Receptors
This Anti-Choline Acetyltransferase Antibody, clone 1.B3.9B3 is validated for use in ELISA, IH, IH(P), WB for the detection of Choline Acetyltransferase.
Western blot

ELISA

Immunohistochemistry: 10-20 μg/mL in paraffin embedded sections {See Ratcliffe et al. 1998}

Optimal working dilutions and protocols must be determined by end user.

Target description

69 kDa

Physical form

Format: Purified
Protein A purified
Purified immunoglobulin. Lyophilized from 0.02 M Phosphate buffer, 0.25 M NaCl with 0.1% sodium azide. Reconstitute to 100 μg/mL with sterile distilled water.

Storage and Stability

Maintain lyophilized antibody at 2–8°C in undiluted aliquots for up to 6 months. Maintain reconstituted antibody at -20°C in undiluted aliquots for up to 6 months.

Analysis Note

Control
Brain tissue

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), 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.

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Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Angela Marina Montalbano et al.
Mediators of inflammation, 2016, 9063842-9063842 (2016-06-15)
IL-17A is overexpressed in the lung during acute neutrophilic inflammation. Acetylcholine (ACh) increases IL-8 and Muc5AC production in airway epithelial cells. We aimed to characterize the involvement of nonneuronal components of cholinergic system on IL-8 and Muc5AC production in bronchial
Production of specific antisera and monoclonal antibodies to choline acetyltransferase: characterization and use for identification of cholinergic neurons.
Eckenstein, F and Thoenen, H
The Embo Journal, 1, 363-368 (1982)
R E Watson et al.
Peptides, 7(1), 155-159 (1986-01-01)
Use of an ethylene glycol based cryoprotectant solution has been found to be effective for the long-term storage of brain tissue either in block form or as freely floating sections prior to immunocytochemical processing. Storage of tissue in the solution
C Ostermann-Latif et al.
Journal of immunological methods, 157(1-2), 73-79 (1993-01-04)
A specific, sensitive, and reliable sandwich-ELISA (enzyme-linked immunosorbent assay) has been established for the determination of choline acetyltransferase (CHAT) from porcine brain. The detection limit of the assay was 30 micrograms/l and the assay was linear up to 300 micrograms/l.
Large-scale purification of choline acetyltransferase and production of highly specific antisera.
Ostermann, C, et al.
European Journal of Biochemistry, 192, 215-218 (1990)

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