Skip to Content
Merck
CN

H2380

6-Hydroxy-DL-DOPA

≥98% (HPLC), powder, APE1 inhibitor

Synonym(s):

2,4,5-Trihydroxy-DL-phenylalanine, 2,5-Dihydroxy-DL-tyrosine

Sign In to View Organizational & Contract Pricing.

Select a Size

About This Item

Empirical Formula (Hill Notation):
C9H11NO5
CAS Number:
21373-30-8
Molecular Weight:
213.19
NACRES:
NA.32
PubChem Substance ID:
24278464
UNSPSC Code:
12352200
MDL number:
MFCD00004272
Beilstein/REAXYS Number:
2860065

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

6-Hydroxy-DL-DOPA, ≥98% (HPLC), powder

InChI

1S/C9H11NO5/c10-5(9(14)15)1-4-2-7(12)8(13)3-6(4)11/h2-3,5,11-13H,1,10H2,(H,14,15)

SMILES string

NC(Cc1cc(O)c(O)cc1O)C(O)=O

InChI key

YLKRUSPZOTYMAT-UHFFFAOYSA-N

assay

≥98% (HPLC)

form

powder

color

off-white

solubility

H2O: 3 mg/mL, 1 M HCl: 50 mg/mL (Solutions should be freshly prepared and protected from exposure to light.)

storage temp.

−20°C

Quality Level

200

Related Categories

General description

Dissolve in oxygen-free boiled water containing 0.1% sodium metabisulfite or other antioxidant. Solutions should be freshly prepared and protected from exposure to light.

Biochem/physiol Actions

Precursor of the catecholaminergic neurotoxin, 6-hydroxydopamine; converted to 6-hydroxydopamine by L-aromatic amino acid decarboxylase.
6-Hydroxy-DL-DOPA is an inhibitor of APE1 (apurinic/apyrimidinic endonuclease) repair-function activity. APE1 is a nuclease crucial for DNA base excision repair pathway. 6-Hydroxy-DL-DOPA also blocks RAD52 (DNA repair protein) single-stranded DNA binding domain.
Precursor 6-hydroxydopamine.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Disclaimer

Hygroscopic; photosensitive

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
BCCN3947
BCCM0465
BCCM5089
BCCL2530
BCCK4047

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Gurushankar Chandramouly et al.
Chemistry & biology, 22(11), 1491-1504 (2015-11-10)
Suppression of RAD52 causes synthetic lethality in BRCA-deficient cells. Yet pharmacological inhibition of RAD52, which binds single-strand DNA (ssDNA) and lacks enzymatic activity, has not been demonstrated. Here, we identify the small molecule 6-hydroxy-DL-dopa (6-OH-dopa) as a major allosteric inhibitor
Mass spectrometric studies of the primary sequence and structure of bovine liver and serum amine oxidase.
G W Adams et al.
Methods in enzymology, 258, 90-114 (1995-01-01)
R M Kostrzewa et al.
Amino acids, 19(1), 183-199 (2000-10-12)
To determine if greater amounts of hydroxyl radical (*OH) are formed by dopamine (DA) denervation and treatment with L-dihydroxyphenylalanine (L-DOPA), the neostriatum was DA denervated (99% reduction in DA content) by 6-hydroxydopamine treatment (134microg icv, desipramine pretreatment) of neonatal rats.
Xiao-Quan Liu et al.
Genes to cells : devoted to molecular & cellular mechanisms, 25(8), 523-537 (2020-05-18)
Although several nucleo(s)tide analogs are available for treatment of HBV infection, long-term treatment with these drugs can lead to the emergence of drug-resistant viruses. Recent HIV-1 studies suggest that combination therapies using nucleo(s)tide reverse transcriptase inhibitors (NRTIs) and non-nucleo(s)tide reverse
A Padiglia et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 4(5), 608-613 (1999-11-07)
The reaction with substrates and carbonyl reagents of native lentil Cu-amine oxidase and its modified forms, i.e. Cu-fully-depleted, Cu-half-reconstituted, Cu-fully-reconstituted, Co-substituted, Ni-substituted and Zn-substituted, has been studied. Upon removal of only one of the two Cu ions, the enzyme loses
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service