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AB120573

L-DOPA, Dopamine (ab120565) precursor

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(9 Publications)

MW 197.19 Da, Purity >99%. Dopamine (ab120565) precursor. Blood-brain barrier permeable. Increases dopamine levels in Parkinson's disease models to display anti-Parkinson's disease properties.

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AML 1, AML1 EVI 1, AML1 EVI 1 fusion protein, AMLCR 1, Acute myeloid leukemia 1, Acute myeloid leukemia 1 protein, Aml1 oncogene, BLM_HUMAN, BS, Bloom syndrome, Bloom syndrome RecQ helicase like, Bloom syndrome protein, CA 1, CA 12, CA 13, CA 14, CA 2, CA IV, CA VA, CA VB, CA-I, CA-II, CA-VI, CA-XII, CA-XIII, CA-XIV, CA13 carbonic anhydrase XIII, CA4, CA5, CA5B, CA6, CAB, CAC, CAH12_HUMAN, CAH13_HUMAN, CAH14_HUMAN, CAH1_HUMAN, CAH2_HUMAN, CAH4_HUMAN, CAH5B_HUMAN, CAH6_HUMAN, CAV, CBF b, CBF-alpha-2, CBF-beta, CBFA 2, Car 1, Car 2, Car4, Carbonate dehydratase I, Carbonate dehydratase II, Carbonate dehydratase IV, Carbonate dehydratase VA, Carbonate dehydratase VB, Carbonate dehydratase VI, Carbonate dehydratase XII, Carbonate dehydratase XIII, Carbonate dehydratase XIV, Carbonic anhydrase 1, Carbonic anhydrase 12, Carbonic anhydrase 13, Carbonic anhydrase 14, Carbonic anhydrase 2, Carbonic anhydrase 4, Carbonic anhydrase 5B, Carbonic anhydrase 5B, mitochondrial, Carbonic anhydrase 6, Carbonic anhydrase A, Carbonic anhydrase B, Carbonic anhydrase B, formerly, Carbonic anhydrase C, Carbonic anhydrase C, formerly, Carbonic anhydrase I, Carbonic anhydrase II, Carbonic anhydrase VA, Carbonic anhydrase VA mitochondrial, Carbonic anhydrase VB, Carbonic anhydrase VB, mitochondrial, Carbonic anhydrase VI, Carbonic anhydrase XII, Carbonic anhydrase XIII, Carbonic anhydrase XIV, Carbonic dehydratase, Carbonic dehydratase IV, Core binding factor alpha 2 subunit, Core binding factor beta subunit, Core binding factor runt domain alpha subunit 2, Core-binding factor subunit alpha-2, Core-binding factor subunit beta, Core-binding factor, beta subunit (CBFB), transcript variant 2, DNA directed DNA polymerase beta, DNA helicase, DNA helicase RecQ like type 2, DNA pol beta, DNA polymerase beta, DNA polymerase beta subunit, DNA polymerase eta, DNA polymerase iota, DPOLB_HUMAN, EC 4.2.1.1, EC=4.2.1.1, ECK0125, Epididymis secretory protein Li 282, Eta 2, FLJ16395, FLJ20151, FLJ21978, GUSTIN, HEL-76, HEL-S-282, HGNC, HSMPP8, HsT18816, JW0122, M-phase phosphoprotein 8, M-phase phosphoprotein, mpp, M-phase phosphoprotein, mpp8, MGC125976, MGC126616, MGC131618, MGC131620, MGC21256, MPHOSPH8, MPP8_HUMAN, OTTHUMP00000108696, OTTHUMP00000108697, OTTHUMP00000108699, OTTHUMP00000108700, OTTHUMP00000108702, Oncogene AML-1, PEA 2, PEA2-alpha B, PEA2-beta, PEBB_HUMAN, PEBP 2B, PEBP2-alpha B, PEBP2-beta, PEBP2A2, PEBP2aB, POLH_HUMAN, POLI_HUMAN, Pol B, Pol beta, Polymerase (DNA directed) beta, Polymerase (DNA directed) iota, Polyomavirus enhancer-binding protein 2 alpha B subunit, Polyomavirus enhancer-binding protein 2 beta subunit, RAD 30B, RAD30, RAD30 homolog A, RAD30 homolog B, RAD30, S. cerevisiae, homolog of, RAD30A, RAD3OB, RECQ 2, RECQ like, RECQL 2, RECQL 3, RP11-523H24.1, RP17, RUNX1_HUMAN, RecQ protein-like 3, RecQ-like type 2, Retinitis pigmentosa 17 (autosomal dominant), Run1, Runt-related transcription factor 1, SL3 3 enhancer factor 1 beta subunit, SL3-3 enhancer factor 1 alpha B subunit, SL3-3 enhancer factor 1 subunit beta, SL3/AKV core-binding factor alpha B subunit, SL3/AKV core-binding factor beta subunit, Salivary carbonic anhydrase, Secreted carbonic anhydrase, T18816, Tumor antigen HOM-RCC-3.1.3, Twa3, Two hybrid-associated protein 3 with RanBPM, UNQ690/PRO1335, XP V, Xeroderma pigmentosum variant type protein, alpha subunit core binding factor, carbonic anhydrase 5A mitochondrial, carbonic anhydrase V mitochondrial, carbonic anhydrase VA mitochondrial1, carbonic anhydrase VI nirs variant 1, carbonic anhydrase VI nirs variant 3, epididymis luminal protein 76, mitochondrial, polymerase DNA directed eta, type 2, yadF

1 Images
Chemical Structure - L-DOPA, Dopamine (ab120565) precursor (AB120573)
  • Chemical Structure

Lab

Chemical Structure - L-DOPA, Dopamine (ab120565) precursor (AB120573)

2D chemical structure image of ab120573, L-DOPA, Dopamine (ab120565) precursor

Key facts

CAS number

5796-17-8

Purity

>99%

Form

Solid

form

Molecular weight

197.19 Da

Molecular formula

C<sub>9</sub>H<sub>1</sub><sub>1</sub>NO<sub>4</sub>

PubChem

92222

Nature

Synthetic

Solubility

Soluble in water to 5 mM

Soluble in 1 eq. HCl to 100 mM

Biochemical name

D-Dopa

Biological description

Dopamine (ab120565) precursor. Blood-brain barrier permeable. Increases dopamine levels in Parkinson's disease models to display anti-Parkinson's disease properties.

Canonical smiles

C1=CC(=C(C=C1CC(C(=O)O)N)O)O

Isomeric smiles

C1=CC(=C(C=C1C[C@H](C(=O)O)N)O)O

InChi

InChI=1S/C9H11NO4/c10-6(9(13)14)3-5-1-2-7(11)8(12)4-5/h1-2,4,6,11-12H,3,10H2,(H,13,14)/t6-/m1/s1

InChiKey

WTDRDQBEARUVNC-ZCFIWIBFSA-N

IUPAC Name

(2R)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DNA polymerase beta also known as POLB is a DNA repair enzyme with a mass of approximately 39 kDa. It is expressed in various tissues with significant levels in the brain and testes. DNA polymerase beta catalyzes the addition of nucleotides to the DNA strand during base excision repair. This process is essential for fixing small-scale damages such as single-nucleotide gaps or uracil bases resulting from spontaneous deamination. Other DNA polymerases of interest include DNA polymerase iota and eta which have specialized roles in replicative and repair functions.
Biological function summary

DNA polymerase beta must maintain genome integrity and stability. It does not operate in isolation but as part of a protein complex involved in recognizing and repairing erroneous DNA base pairing. DNA polymerase iota is also a member of the DNA polymerase family operating differently by introducing errors selectively which is sometimes beneficial in bypassing DNA lesions. The carbonic anhydrase family including CA2 CA1 and other forms plays a role in catalyzing the reversible hydration of carbon dioxide essential for maintaining acid-base balance. Each member of this family such as CA4 and CA12 has distinct tissue distributions and specific roles.

Pathways

DNA polymerase beta contributes significantly to the base excision repair (BER) pathway a critical pathway for repairing minor DNA damage. The BER pathway involves several proteins including PARP (poly ADP-ribose polymerase) which detects DNA strand breakage and recruits other repair enzymes including POLB. The pathway regulates DNA stability within both normal physiological processes and in response to chemical damage. In contrast the carbonic anhydrases are involved in bicarbonate transport pathways important for processes like respiration and renal acid-base regulation.

Defects in DNA polymerase beta activity can lead to neurodegenerative diseases and cancer as DNA repair mechanisms fail allowing mutations to accumulate. Similarly Bloom syndrome protein Blm which interacts with DNA repair pathways if mutated leads to Bloom syndrome characterized by genomic instability and increased cancer risk. Additionally mutations in carbonic anhydrases like CA12 and CA5B are linked to disorders affecting the kidneys and skeletal system due to their roles in maintaining pH balance. RUNX1 vital for hematopoiesis when altered relates to certain types of leukemia indicating the significant impact of these proteins on human health.

Product protocols

Publications (9)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 26: PubMed40076918

2025

Widespread and Heterologous Effects of L-DOPA on Monoaminergic Tissue Metabolism in Newborn Rats Expressing Air-Stepping.

Applications

Unspecified application

Species

Unspecified reactive species

Grégory Barrière,Zora Pelloquin-Mvogo,Marie Boulain,Inès Khsime,Rahul Bharatiya,Marie-Anne Riquier,Didier Morin,Anne-Emilie Allain,Abdeslam Chagraoui,Laurent Juvin,Philippe De Deurwaerdere

International journal of molecular sciences 24: PubMed37834195

2023

Limiting Monoamines Degradation Increases L-DOPA Pro-Locomotor Action in Newborn Rats.

Applications

Unspecified application

Species

Unspecified reactive species

Inès Khsime,Marie Boulain,Abderrahman Fettah,Abdeslam Chagraoui,Gilles Courtand,Philippe De Deurwaerdère,Laurent Juvin,Grégory Barrière

The Journal of physiology 599:4455-4476 PubMed34411301

2021

L-DOPA and 5-HTP modulation of air-stepping in newborn rats.

Applications

Unspecified application

Species

Unspecified reactive species

Marie Boulain,Wei Yuan,Zied Oueghlani,Inès Khsime,Vianney Salvi,Gilles Courtand,Christophe Halgand,Didier Morin,Philippe de Deurwaerdere,Grégory Barrière,Laurent Juvin

Genes & development 34:37-52 PubMed31831628

2019

Muscle-derived Dpp regulates feeding initiation via endocrine modulation of brain dopamine biosynthesis.

Applications

Unspecified application

Species

Unspecified reactive species

Maricela Robles-Murguia,Deepti Rao,David Finkelstein,Beisi Xu,Yiping Fan,Fabio Demontis

Cell 174:481-496.e19 PubMed30007419

2018

A Genetically Encoded Fluorescent Sensor Enables Rapid and Specific Detection of Dopamine in Flies, Fish, and Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Fangmiao Sun,Jianzhi Zeng,Miao Jing,Jingheng Zhou,Jiesi Feng,Scott F Owen,Yichen Luo,Funing Li,Huan Wang,Takashi Yamaguchi,Zihao Yong,Yijing Gao,Wanling Peng,Lizhao Wang,Siyu Zhang,Jiulin Du,Dayu Lin,Min Xu,Anatol C Kreitzer,Guohong Cui,Yulong Li

Frontiers in pharmacology 8:700 PubMed29046640

2017

Antiparkinsonian Efficacy of Guanosine in Rodent Models of Movement Disorder.

Applications

Unspecified application

Species

Unspecified reactive species

Caio M Massari,Marc López-Cano,Fabiana Núñez,Víctor Fernández-Dueñas,Carla I Tasca,Francisco Ciruela

Scientific reports 7:9181 PubMed28835637

2017

Cutaneous pigmentation modulates skin sensitivity via tyrosinase-dependent dopaminergic signalling.

Applications

Unspecified application

Species

Unspecified reactive species

Kentaro Ono,Chi T Viet,Yi Ye,Dongmin Dang,Suzuro Hitomi,Takashi Toyono,Kiyotoshi Inenaga,John C Dolan,Brian L Schmidt

Scientific reports 5:16823 PubMed26592948

2015

Plant phenolics are detoxified by prophenoloxidase in the insect gut.

Applications

Unspecified application

Species

Unspecified reactive species

Kai Wu,Jie Zhang,Qiaoli Zhang,Shoulin Zhu,Qimiao Shao,Kevin D Clark,Yining Liu,Erjun Ling

Disease models & mechanisms 8:57-63 PubMed25398851

2014

Untangling dopamine-adenosine receptor-receptor assembly in experimental parkinsonism in rats.

Applications

Unspecified application

Species

Unspecified reactive species

Víctor Fernández-Dueñas,Jaume J Taura,Martin Cottet,Maricel Gómez-Soler,Marc López-Cano,Catherine Ledent,Masahiko Watanabe,Eric Trinquet,Jean-Philippe Pin,Rafael Luján,Thierry Durroux,Francisco Ciruela
View all publications

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