Dopamine beta-Hydroxylase cDNA ORF Clone in Cloning Vector, Human

Cat: HG13440-G
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Dopamine beta-Hydroxylase cDNA ORF Clone in Cloning Vector, Human General Information
NCBI Ref Seq
RefSeq ORF Size
1812 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence.
Full length Clone DNA of Human dopamine beta-hydroxylase (dopamine beta-monooxyge).
pGEM-T Vector
Sequencing Primers
SP6 and T7 or M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
Dopamine beta-Hydroxylase cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

Dopamine beta-Hydroxylase cDNA ORF Clone in Cloning Vector, Human Alternative Names
DBM cDNA ORF Clone, Human
Dopamine beta-Hydroxylase Background Information

DBH is a 290 kDa copper-containing oxygenase. It can be detected in noradrenergic nerve terminals of the central and peripheral nervous systems, and is also expressed in chromaffin cells of the adrenal medulla. DBH contains our identical subunits, and its activity requires ascorbate as a cofactor. It functions in in the synthesis of small-molecule neurotransmitters that is membrane-bound, making norepinephrine the only transmitter synthesized inside vesicles. DBH has been shown to be associated with decision making and addictive behaviors such as alcohol and smoking, attention deficit hyperactivity disorder, and also with neurological diseases such as Schizophrenia and Alzheimer's.

Full Name
dopamine beta-hydroxylase (dopamine beta-monooxygenase)
  • Rush RA. et al., 1980, Crit Rev Clin Lab Sci. 12 (3): 241-77.
  • Goldstein M. et al., 1964, Life Sci. 3 (7): 763-7.
  • S Friedman. et al., 1966, The Journal of Biological Chemistry. 241 (10): 2256-9.
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