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Choline Acetyltransferase Recombinant Rabbit monoclonal Antibody IgG

SKU: BA112217-100µl
$279.00Price

Fig1: ICC staining Cho

  Line Acetyltransferase in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig2: ICC staining Choline Acetyltransferase in N2A cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig3: ICC staining Choline Acetyltransferase in SH-SY5Y cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Bon Opus Cat. #BA112217
Size
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Recombinant protein
  • Application Summary

    WB, IP, ICC/IF, IHC, FC
  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Choline O-acetyltransferase
  • Background

    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.(ET1704-16)