Anti-Choline Acetyltransferase antibody
Specifications
| Product type: | Primary antibody |
| Antigen: | Choline Acetyltransferase |
| Immunogen: | Recombinant protein |
| Species immunized: | Rabbit |
| Isotype: | IgG |
| Applications: | Western Blot (1:400-1:1000); Immunohistochemistry (1:40-1:200); Flow Cytometry (1:40-1:100); Immunocytochemistry (1:40-1:200); Immunoprecipitation (1:15-1:50); Immunofluorescence |
| Reactivity: | Human, Mouse, Rat |
| Clonality (clone number): | Monoclonal (JA67-11) |
| Form: | Liquid |
| Buffer: | Tris-HCl buffer (pH7.4), 1% BSA, 40% glycerol, 0.05% NaN3. |
| Concentration: | 1mg/ml |
| Purity: | Protein A affinity purified |
| Storage: | Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles. |
| Alternative names: | Acetyl CoA choline O acetyltransferase antibody |
| Acetyl CoA:choline O acetyltransferase antibody | |
| ChAT antibody | |
| CHOACTase antibody | |
| Choline acetylase antibody | |
| Choline acetyltransferase antibody | |
| Choline O acetyltransferase antibody | |
| Choline O-acetyltransferase antibody | |
| CLAT_HUMAN antibody | |
| CMS1A antibody | |
| CMS1A2 antibody | |
| EC 2.3.1.6 antibody | |
| OTTHUMP00000019583 antibody | |
| OTTHUMP00000019584 antibody |
Target information
Choline acetyltransferase (also designated choactase, choline O-acetyltransferase) synthesizes acetylcholine in cholinergic neurons. Multiple choactase mRNAs with different 5′-noncoding regions are expressed as R-, N1, N2-, S- and M-types. N1-, N2- and R-type mRNAs produce a single short enzyme, while M-type mRNA produces both long and short enzymes. The long enzyme is targeted to the nuclei of cells, whereas the short protein is found in cytoplasm. A novel NFkB binding site is located within the nerve growth factor-responsive enhancer element that is recognized by the NFkB protein p49, but not p65 or p50. Decreased choactase expression and increased NFkB activity are associated with aging and Alzheimer’s disease, indicating that p49 is a negative regulator of choactase expression and suggesting a possible mechanism for aging-associated declines in cholinergic function. Phosphorylation of choactase has been shown to enhance choactase catalytic activity. Specifically, Serine 440 is found to be the phosphorylation site in a recombinant human short choactase by protein kinase C and is involved in regulation of the enzyme catalytic activity and binding to subcellular membranes.
Provider
Erpantech Laboratory