Monoclonal antibodies to choline acetyltransferase
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Monoclonal antibodies to choline acetyltransferase production, specificity, and immunohistochemistry by Allan I. Levey

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Published .
Written in English

Book details:

Edition Notes

Statementby Allan I. Levey.
LC ClassificationsMicrofilm 83/181 (R)
The Physical Object
Paginationvii, 137 leaves
Number of Pages137
ID Numbers
Open LibraryOL3273853M
LC Control Number83196564

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Monoclonal antibodies selective for rat brain choline acetyltransferase (acetyl-CoA: choline O-acetyltransferase, EC ) were prepared by standard techniques. Five cell lines were isolated from spleen cell-SP/2 hybrids by repetitive cloning with a screening Cited by: This paper has described experimental approaches for the development and application of monclonal antibodies against the specific cholinergic marker, choline acetyltransferase. Since ChAT was a difficult enzyme to purify, a strategy was developed for detecting the presence of specific antibodies when impure antigen preparations were used for Author: Bruce H. Wainer, Allan I. Levey, Elliott J. Mufson, M. Marsel Mesulam. Choline acetyltransferase (commonly abbreviated as ChAT, but sometimes CAT) is a transferase enzyme responsible for the synthesis of the neurotransmitter acetylcholine. ChAT catalyzes the transfer of an acetyl group from the coenzyme acetyl-CoA to choline, yielding acetylcholine (ACh).BRENDA: BRENDA entry. Each Choline Acetyltransferase/ChAT Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. Our Choline Acetyltransferase/ChAT Antibodies can be used in a variety of model species: Chicken, Guinea Pig, Human, Mouse, Primate, Rat.

Four monoclonal antibodies were obtained to rat brain choline acetyltransferase (CAT). The enzyme was purified 95,fold from rat brain by precipitation with acetic acid at pH , fractionation with 40 to 60% (NH&S04, CM-Sephadex chromatography, and affinity column chromatography on Cited by: Monoclonal antibodies to rat striatal choline acetyltransferase were produced by fusion of sensitized mouse lymphocytes with murine plasmacytoma (NS1) cells. Two stable anti-choline acetyltransferase lines were established by limiting dilution cloning. Specificity of Cited by: This is a Validated Antibody Database (VAD) review about human choline acetyltransferase, based on published articles (read how Labome selects the articles), using choline acetyltransferase antibody in all is aimed to help Labome visitors find the most suited choline acetyltransferase antibody. The protein, choline acetyltransferase (ChAT; EC ), was analyzed in wild-type and two different temperature-sensitive ChAT mutants of Drosophila (Cha ts1 and Cha ts2) using newly generated monoclonal all of the three genotypes, Western blots of crude fly head extracts showed a band stained at approximately the kDa position, supporting the hypothesis that these Cited by:

Mouse anti Rat choline acetyltransferase antibody, clone 1E6 recognizes choline acetyltransferase and stains cholinergic neurons in the brain and central nervous system. Choline acetyltransferase is an enzyme, present the presynaptic ends of axons, that catalyzes the transfer of the acetyl group of acetyl CoA to choline, forming the neurotransmitter acetylcholine. Anti-Choline Acetyltransferase Antibody is an antibody against Choline Acetyltransferase for use in IH & WB. Synonym: ChAT [email protected] NACRES NA SDS Purchase Primary, Secondary and Recombinant Monoclonal Antibodies Providing highly cited primary and secondary antibodies, we have you covered for your ELISA, western blot. The Journal of Neuroscience Specific Localization of ChA.T with Monoclonal Antibodies 3 brain. Male Sprague-Dawley rats ( to grn) were slices were made with a razor blade throughout the entire anesthetized with pentobarbital(50 mg/kg) and perfused rostrocaudal extent of the brain and subsequently wereCited by: Rabbit recombinant monoclonal Choline Acetyltransferase antibody [EPR]. Validated in WB, IHC and tested in Mouse, Rat, Rabbit, Guinea pig. Cited in 7 publication(s). Independently reviewed in 4 5/5(4).