Choline O-Acetyltransferase (CHAT) (C-Term) Antikörper

Antigen: Choline O-Acetyltransferase (CHAT)

Synonyme: CMS1A, CMS1A2, B230380D24Rik, CT23399, Cat, ChAT, cha, dChAT, l(3)91Cc, DmelCG12345, CG12345, CHAT, ChoAcTase, Ci-ChAT

Epitope: C-Term

Klonalität: Polyklonal

Wirt: Kaninchen

Applikation: Immunhistochemie (IHC), Western Blot (WB)

Produktnummer: ABIN350209

Produktbeschreibung

Weitere Bezeichnung: ChAT (choline O-acetyltransferase) (c-terminal region)

Swiss-Prot: P32738

Immunogen: A synthetic peptide as a part of rat and mouse ChAT (choline O-acetyltransferase) conjugated to an immunogenic carrier protein was used as the immunogen.

Format: Lyophilized

Beschreibung: Cholinergic systems are implicated in numerous neurologic functions. Alteration in some cholinergic neurons may account for the disturbances of Alzheimer disease. The protein encoded by this gene synthesizes the neurotransmitter acetylcholine. Alternative splice variants have been found that contain alternative 5' untranslated exons. Three of the four described splice variants encode identical 69 kDa proteins while one variant encodes both the 69 kDa and a larger 82 kDa protein. Choline acetylase  catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine. Defects in CHAT are the cause of familial infantile myasthenia gravis 2 (FIMG2); also known as CMS-EA. FIMG2 patients have myasthenic symptoms since birth or early infancy, negative tests for anti-AChR antibodies, and abrupt episodic crises with increased weakness, bulbar paralysis, and apnea precipitated by undue exertion, fever, or excitement. Inheritance is autosomal recessive. Also known as: CHOACTase, choline acetylase, choline O-acetyltransferase, CMS1A, CMS1A2, B230380D24Rik.

Spezifität: Appears to be specific for ChAT.

Anwendungen

Applikationshinweise: IHC, WB. A dilution of 1: 300 to 1: 2000 is recommended. The optimal dilution should be determined by the end user.

Reinheit: whole serum

Lagerung: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

IF on 1 day- old mouse cortical cell culture using Rabbit antibody to rat, mouse ChAT (choline O-acetyltransferase): whole serum (ABIN350209) at 1: 2000 dilution. DAPI counter stained.

IF on 1 day- old mouse cortical cell culture using Rabbit antibody to rat, mouse ChAT (choline O-acetyltransferase): whole serum (ABIN350209) at 1: 2000 dilution. DAPI counter stained.

IHC on rat spinal cord using Rabbit antibody to rat, mouse ChAT (choline O-acetyltransferase): whole serum (ABIN350209) at 1 : 2000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the immunostaining (not shown).

Publikationen

Publikationen: Ishii, Oda, Ichikawa et al.: "Complementary DNAs for choline acetyltransferase from spinal cords of rat and mouse: nucleotide sequences, expression in mammalian cells, and in situ hybridization." in: Brain research. Molecular brain research, Vol. 7, Issue 2, pp. 151-9, 1990 (PubMed).

Wu, Hersh: "Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis." in: The Journal of biological chemistry, Vol. 270, Issue 49, pp. 29111-6, 1996 (PubMed).

Kengaku, Misawa, Deguchi: "Multiple mRNA species of choline acetyltransferase from rat spinal cord." in: Brain research. Molecular brain research, Vol. 18, Issue 1-2, pp. 71-6, 1993 (PubMed).

Cai, Cronin, Engel et al.: "Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders." in: The EMBO journal, Vol. 23, Issue 10, pp. 2047-58, 2004 (PubMed).

Govindasamy, Pedersen, Lian et al.: "Structural insights and functional implications of choline acetyltransferase." in: Journal of structural biology, Vol. 148, Issue 2, pp. 226-35, 2004 (PubMed).