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MABN1773

Sigma-Aldrich

Anti-oxDJ-1 Antibody (Cys106), clone M149

clone M149, from mouse

Synonym(s):

Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, oxDJ-1 (Cys106)

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M149, monoclonal

species reactivity

mouse, human

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... PARK7(11315)

Related Categories

General description

Protein DJ-1 (UniProt Q99497; also known as Parkinson disease (autosomal recessive, early onset) protein 7, Epididymis secretory sperm binding protein Li 67p, Oncogene DJ1) is encoded by the PARK7 (also known as DJ1, HEL-S-67p) gene (Gene ID 11315) in human. DJ-1 belongs to the ThiJ/PfpI family of proteins characterized by a ThiJ domain. DJ-1 is reported to be involved in multiple physiological processes, including cellular oncogenic transformation, RNA-protein interaction regulation, sperm fertilization, antioxidative defense, and transcriptional regulation. Mutations in the DJ-1 gene, PARK7, are known causes of autosomal recessive parkinsonism with a clinical presentation similar to other forms of recessive PD syndromes. DJ-1 cysteine residue 106 (Cys106) is preferentially oxidized through direct oxygen addition in response to cellular oxidative stress. Cysteine forms 3 different oxidized species, cysteine–sulfenic acid (Cys-SOH), cysteine–sulfinic acid (Cys-SO2H), and cysteine–sulfonic acid (Cys-SO3H). The Cys-SO2H form of oxDJ-1 is likely the active form, and further oxidation to Cys-SO3H leads to loss of biologic function. The levels of oxDJ-1 in erythrocytes from unmedicated PD patients are reported to be markedly higher than those from medicated PD patients and healthy subjects.

Specificity

Immunoreactivity toward Cys-SO2H or Cys-SO3H form of oxDJ-1 is not yet determined.

Immunogen

Epitope: Cys106-SO2H/-SO3H
His-tagged oxidized recombinant DJ-1 purified from H2O2-treated E. coli host corresponding to the Cys106-SO2H/-SO3H of human oxDJ-1.

Application

Immunohistochemistry: A reporesentative lot detected DJ-1 oxidation in various regions of murine (cerebral cortex, hippocampus, striatum, SN pars compacta, SN pars reticulata) and human (SN and red nucleus of the midbrain) brain tissue sections (Saito, Y., et al. (2014). J Neuropathol Exp Neurol. 73(7):714-728.)
Western Blotting Analysis: A reporesentative lot detected basal DJ-1 oxidation (oxDJ-1) in human neuroblastoma SH-SY5Y cells and murine fibroblasts from wild-type, but not DJ-1 knockout, mice, as well as enhanced oxDJ-1 in H2O2-treated SH-SY5Y cells (Saito, Y., et al. (2014). J Neuropathol Exp Neurol. 73(7):714-728.).
Research Category
Neuroscience
Research Sub Category
Developmental Signaling
This Anti-oxDJ-1 Antibody (Cys106), clone M149 is validated for use in Western Blotting and Immunohistochemistry for the detection of oxDJ-1.

Quality

Evaluated by Western Blotting in SH-SY5Y cell lysate.

Western Blotting Analysis: 0.1 µg/mL of this antibody detected enhanced DJ-1 oxidation in 10 µg cell lysate from H2O2-treated human neuroblastoma SH-SY5Y cells.

Target description

~20 kDa observed. Uncharacterized band(s) may appear in some lysates.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Rui Sun et al.
Molecular & cellular proteomics : MCP, 16(10), 1789-1800 (2017-08-18)
4-Oxo-2-nonenal (ONE) derived from lipid peroxidation modifies nucleophiles and transduces redox signaling by its reactions with proteins. However, the molecular interactions between ONE and complex proteomes and their dynamics in situ remain largely unknown. Here we describe a quantitative chemoproteomic
Diana A Quintero-Espinosa et al.
Environmental toxicology, 37(3), 660-676 (2021-12-14)
It is increasingly evident that LRRK2 kinase activity is involved in oxidative stress (OS)-induced apoptosis-a type of regulated cell death and neurodegeneration, suggesting LRRK2 inhibition as a potential therapeutic target. We report that a phenolic-rich extract of avocado Persea americana
Yuichiro Mita et al.
Scientific reports, 8(1), 12056-12056 (2018-08-15)
DJ-1 plays an important role in antioxidant defenses, and a reactive cysteine at position 106 (Cys106) of DJ-1, a critical residue of its biological function, is oxidized under oxidative stress. DJ-1 oxidation has been reported in patients with Parkinson's disease
Diana Alejandra Quintero-Espinosa et al.
International journal of molecular sciences, 24(13) (2023-07-14)
Leucine-rich repeat kinase 2 (LRRK2) has been linked to dopaminergic neuronal vulnerability to oxidative stress (OS), mitochondrial impairment, and increased cell death in idiopathic and familial Parkinson's disease (PD). However, how exactly this kinase participates in the OS-mitochondria-apoptosis connection is
Katalin Solti et al.
Neurobiology of disease, 134, 104629-104629 (2019-11-02)
The loss of native function of the DJ-1 protein has been linked to the development of Parkinson's (PD) and other neurodegenerative diseases. Here we show that DJ-1 aggregates into β-sheet structured soluble and fibrillar aggregates in vitro under physiological conditions

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