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XPS-2000


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Primary Antibodies

Dopamine Decarboxylase Antibody

Background

Aromatic L-amino acid decarboxylase (AADC; DOPA decarboxylase; DDC) catalyzes the second reaction in the biosynthesis of catecholamines and serotonin. It is also involved in the biosynthesis of trace amines.

Dopamine Decarboxylase Antibody

Description

Left: Dopamine Decarboxylase Antibody

Purification

Affinity purified

Clonality / Clone

This is a polyclonal antibody.

Host

Dopamine Decarboxylase antibody was raised in rabbit.

Please use anti-rabbit secondary antibodies.

Immunogen

Rabbit anti-DOPA Decarboxylase polyclonal antibody was raised against a SDS denatured, recombinant bovine aromatic DDC expressed in E. coli and purified from inclusion bodies. Rabbit anti-DOPA Decarboxylase was prepared from rabbit serum by affinity purification using an AminoLink Plus column matrix to which purified, recombinant bovine DDC was coupled.

Application

Dopamine Decarboxylase antibody is specific immunolabeling of the ~55k DDC protein in Western blots of rat adrenal medulla. Applications include Dot Blots (DB) and Western Blots (WB). Recognizes DDC in rat adrenal medulla and caudate. When internally tested under ideal conditions the working dilutions were 1:1000 for DB and WB.

Tested Application

WB

Buffer

Dopamine Decarboxylase antibody is supplied as affinity purified polyclonal antibody, 100 μl in 150 mM NaCl, 10 mM HEPES, 100 μg per ml BSA and 50% glycerol, pH 7.5., and there is adequate amount of material to conduct 10-mini Western Blots.

Storage

For long term storage –80˚C is recommended, but shorter term storage at –20˚C is also acceptable as aliquots may be taken without freeze/thawing due to the presence of 50% glycerol. Stable for one year.

Species Reactivity

R, B

This product belongs to the following categories:

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References

  1. Haycock, J.W., Becker, L., Ang, L., Furukawa, Y., Hornykiewicz, O., and Kish, S.J., “Marked disparity between age-related changes in dopamine and other presynaptic dopaminergic markers in human striatum,” J. Neurochem. 87 (2003) 574 - 585.
  2. Waymire, J.C. and Haycock, J.W. “Lack of regulation of aromatic L-amino acid decarboxylase in intact bovine chromaffin cells,” J. Neurochem. 81 (2002) 589 - 593.
  3. Berry, M.D., Juorio, A.V., Li, X.M., and Boulton, A.A. “Aromatic L-amino acid decarboxylase: a neglected and misunderstood enzyme,” Neurochem. Res. 21 (1996) 1075 -1087.


Datasheet 0802-W

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