|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||63365 Da|
|Homology||Rat, human - 12/13 amino acid residues identical.|
|Other Names||High affinity choline transporter 1, Hemicholinium-3-sensitive choline transporter, CHT, Solute carrier family 5 member 7, Slc5a7, Cht1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DWNQTAYGYPDPK, corresponding to amino acid residues 299-311 of mouse Choline Transporter (Accession Q8BGY9). 4th extracellular loop.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
In cholinergic neurons, acetylcholine is synthesized from choline and acetyl-coenzyme A (acetyl-CoA). Following depolarization, acetylcholine is released in the synaptic cleft via synaptic vesicles and activates muscarinic and nicotinic receptors located on postsynaptic membranes1,2. Acetylcholine released in the synaptic cleft is rapidly hydrolyzed into choline and acetate. Since choline is not de novo synthesized and thereby only made available through diet uptake, choline is recycled back into the cells in order to regenerate acetylcholine. For this purpose, choline is taken up by the high affinity choline transporter (CHT)1,2. CHT has thirteen transmembrane domains, an extracellular N-terminus and an intracellular C-terminus3,4. CHT belongs to the Na+-dependent glucose transporter family (SLC5). The activity of the transporter can be confirmed by its sensitivity to hemicholimium-3 (HC-3) which inhibits the transport of choline with a Ki of 10-100 nM1. The activity of CHT reflects that of neurons1,5 i.e., increased CHT activity indicates an increase in neuronal activity. The increase in the activity of the transporter is due to the increase in the number of transporters and not due to the increase in activity per se. In addition CHT activity is also regulated by second messengers. Phosphorylation of the transporter also seems to determine the activity as it has many consensus phosphorylation sites present in the C-terminal1,2. Expression studies reveal that CHT is expressed solely in cholinergic neurons making the transporter a useful marker for detecting these types of neurons5. Abgent is pleased to offer a highly specific antibody directed against an epitope of mouse CHT. Anti-Choline Transporter (CHT) (extracellular) antibody (#AG1292) can be used in western blot analysis and immunocytochemistry applications. It has been designed to recognize CHT from rat, mouse and human samples.
References 1. Ribeiro, F.M. et al. (2006) J. neurochem. 97, 1. 2. Okuda, T. and Haga, T. (2003) Neurochem. Res. 28, 483. 3. Apparsundaram, S. et al. (2000) Biochem. Biophys. Res. Commun. 276, 862. 4. Ferguson, S.M. and Blakely, R.S. (2004) Mol. Intervent. 4, 22. 5. Simon, J.R. and Kuhar, M.G. (1975) Nature 255, 162. 6. Misawa, H. et al. (2001) Neuroscience 105, 87.
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