Dopa Decarboxylase (Aromatic L-Amino Acid Decarboxylase) (DDC) (AA 1-480), (full length) (Active) protein (His tag)

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Protein Name
  • 5-HT
  • AADC
  • CG10697
  • DDC
  • DdcDm
  • Dmel\\CG10697
  • ddc
  • fDDC
  • l(2)37Bl
  • l(2)37Ch
  • l(2)k02104
  • AMD-r
  • CG10501
  • CG17345
  • Dmel\\CG10501
  • X04695
  • fAMD
  • l(2)37Bk
  • l(2)amd
  • l(2)amd alpha-methyldopa hypersensitive
  • l(2)amd[H]
  • Ddc
  • DdcDv
  • Dvir\\GJ17995
  • GJ17995
  • dvir_GLEANR_2561
  • wu:fa56d05
  • wu:fd59h03
  • wu:fk20h01
  • zgc:65801
  • zgc:76929
  • Aadc
  • Dopa decarboxylase
  • alpha methyl dopa-resistant
  • dopa decarboxylase (aromatic L-amino acid decarboxylase)
  • dopa decarboxylase
  • Dopa-decarboxylase
  • Ddc
  • amd
  • DDC
  • ddc
  • Dvir\\Ddc
Protein Characteristics
AA 1-480, full length
8
1
1
1
1
1
1
1
1
Origin
Human
14
2
1
1
1
1
Source
Baculovirus infected Insect Cells
4
4
3
2
2
1
Protein Type
Recombinant
Biological Activity
Active
Purification tag / Conjugate
This DDC protein is labelled with His tag.
Application
Functional Studies (Func), SDS-PAGE (SDS)
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Characteristics The recombinant human DDC consists of 490 amino acids and predicts a molecular mass of 55 kDa. It migrates as an approximately 48 kDa protein in SDS-PAGE under reducing conditions.

Protein Structure: A DNA sequence encoding the full length of human DDC (NP_000781.1) (Met 1-Glu 480) was expressed with a polyhistidine tag at the C-terminus.
Predicted N-Term: Met
Purity > 90 % as determined by SDS-PAGE
Endotoxin Level < 1.0 EU per μg of the protein as determined by the LAL method
ProductDetails: Biological Activity Comment Measured by its ability to convert the substrate 3, 4-dihydroxy L-phenylalanine (L-Dopa) to 3, 4-dihydroxyphenylethylamine (dopamine). The dopamine product is measured by its absorbance at 340 nm after derivatization with trinitrobenzene sulfonic acid . The specific activity is >1500 pmoles/min/μg .
Background Synonyms: AADC
Molecular Weight 55 kDa, 48 kDa
NCBI Accession NP_000781
Pathways Dopaminergic Neurogenesis
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Format Liquid
Buffer Supplied as sterile 50 mM Tris, 100 mM NaCl, pH 8, 10 % glycerol
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
Handling Advice Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Storage -20 °C,-80 °C
Storage Comment Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping: Liquid. It is shipped out with blue ice.
Expiry Date 12 months
Supplier Images
 image for Dopa Decarboxylase (Aromatic L-Amino Acid Decarboxylase) (DDC) (AA 1-480), (full length) (Active) protein (His tag) (ABIN3216385) Dopa Decarboxylase (Aromatic L-Amino Acid Decarboxylase) (DDC) (AA 1-480), (full length) (Active) protein (His tag)
Background publications Vassilacopoulou, Sideris, Vassiliou, Fragoulis: "Identification and characterization of a novel form of the human L-dopa decarboxylase mRNA." in: Neurochemical research, Vol. 29, Issue 10, pp. 1817-23, 2004

Vassilacopoulou, Sideris, Vassiliou, Fragoulis: "Identification and characterization of a novel form of the human L-dopa decarboxylase mRNA." in: Neurochemical research, Vol. 29, Issue 10, pp. 1817-23, 2004 (PubMed).

Moore, Dominici, Borri Voltattorni: "Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes." in: The Biochemical journal, Vol. 315 ( Pt 1), pp. 249-56, 1996

Moore, Dominici, Borri Voltattorni: "Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes." in: The Biochemical journal, Vol. 315 ( Pt 1), pp. 249-56, 1996 (PubMed).

Scherer, McPherson, Wasmuth, Marsh: "Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs." in: Genomics, Vol. 13, Issue 2, pp. 469-71, 1992 (PubMed).

Ichinose, Kurosawa, Titani, Fujita, Nagatsu: "Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase." in: Biochemical and biophysical research communications, Vol. 164, Issue 3, pp. 1024-30, 1989

Ichinose, Kurosawa, Titani, Fujita, Nagatsu: "Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase." in: Biochemical and biophysical research communications, Vol. 164, Issue 3, pp. 1024-30, 1989 (PubMed).