MABN1773
Anti-oxDJ-1 Antibody (Cys106), clone M149
clone M149, from mouse
Sinónimos:
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
Productos recomendados
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)
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.).
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
Neuroscience
Research Sub Category
Developmental Signaling
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.
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
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Rui Sun et al.
Molecular & cellular proteomics : MCP, 16(10), 1789-1800 (2017-08-18)
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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
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
Viviana Soto-Mercado et al.
PloS one, 15(5), e0221669-e0221669 (2020-05-22)
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive memory loss and cognitive disturbance as a consequence of the loss of cholinergic neurons in the brain, neuritic plaques and hyperphosphorylation of TAU protein. Although the underlying mechanisms leading to
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