Product nameAnti-PARK7/DJ1 antibody [MJF-R16 (66-5)] - Oxidized
See all PARK7/DJ1 primary antibodies
DescriptionRabbit monoclonal [MJF-R16 (66-5)] to PARK7/DJ1 - Oxidized
SpecificityThis antibody detects the oxidised form of the Park7 protein.
Tested applicationsSuitable for: WBmore details
Unsuitable for: ICC/IF or IHC-P
Species reactivityReacts with: Human
Synthetic peptide corresponding to Human PARK7/DJ1 aa 100-200.
Database link: Q99497
- HeLa whole cell lysate (ab150035), treated with hydrogen peroxide.
In recent years, a critical need in the Parkinson's Disease (PD) research community has been access to well-characterized antibodies directed against known PD-relevant proteins. The Michael J. Fox Foundation (MJFF) has supported this effort by partnering with Drs. Un Kang and David White (University of Chicago) to help accelerate PD research.
DJ-1 is widely expressed in the adult mammal and highly conserved between species. Loss-of-function mutations in DJ-1 were recently identified in an autosomal recessive form of Parkinson’s disease (PARK7). Among other roles, DJ-1 protects cells against oxidative stress. Oxidization of the cysteine 106 residue (C106) of DJ-1 occurs as a consequence oxidative stress, but is also necessary to fully activate DJ-1 functions. The oxidation state of DJ-1 C106 appears to lead to distinct roles for DJ-1 in the cellular response to oxidative stress. Oxidation of C106 to the sulfinic (-SO2H) form has been implicated as a necessary step to achieve optimal protective functions of DJ-1, whereas oxidation to the sulfonic form (-SO3H) results in the oxidative destabilization of DJ-1 structure. The sulfonic form has been identified as a major oxidized form in PD brains.
With the generation of this critical research tool, MJFF hopes to ensure that the role of this modification can be further investigated by all researchers and the relevance of oxidized forms of DJ-1 can be more definitively examined in Parkinson’s disease.
Rat: We have preliminary internal testing data to indicate this antibody may not react with these species. Please contact us for more information.
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.01% Sodium azide
Constituents: 50% Glycerol, 0.05% BSA
Concentration information loading...
PurityProtein A purified
Clone numberMJF-R16 (66-5)
Our Abpromise guarantee covers the use of ab169520 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000 - 1/10000. Predicted molecular weight: 20 kDa.|
FunctionProtects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.
Tissue specificityHighly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain. Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa.
Involvement in diseaseDefects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:606324]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).
Sequence similaritiesBelongs to the peptidase C56 family.
modificationsSumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.
Cys-106 is easily oxidized to sulfinic acid.
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.
Cellular localizationCytoplasm. Nucleus. Mitochondrion. Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Detected in tau inclusions in brains from neurodegenerative disease patients.
- Information by UniProt
- CAP1 antibody
- DJ-1 antibody
- DJ1 antibody
All lanes : Anti-PARK7/DJ1 antibody [MJF-R16 (66-5)] - Oxidized (ab169520) at 1/10000 dilution (purified)
Lane 1 : Untreated HeLa whole cell lysate
Lane 2 : HeLa whole cell lysate treated with hydrogen peroxide
Lysates/proteins at 10 µg per lane.
All lanes : Goat Anti-Rabbit IgG H&L (HRP) (ab97051) at 1/20000 dilution
Predicted band size: 20 kDa
Observed band size: 23 kDa why is the actual band size different from the predicted?
Blocking buffer: 5% NFDM/TBST
Dilution buffer: 5% NFDM/TBST
All lanes : Anti-PARK7/DJ1 antibody [MJF-R16 (66-5)] - Oxidized (ab169520) at 1/1000 dilution (Unpurified)
Lane 1 : HeLa cell lysate, untreated
Lane 2 : HeLa cell lysate, treated with hydrogen peroxide
Lysates/proteins at 10 µg per lane.
All lanes : Goat anti-rabbit HRP at 1/2000 dilution
Predicted band size: 20 kDa
ab169520 highlights the presence or absence of the oxidized form of this protein; an antibody directed against total PARK7/DJ1 illustrates the presence of PARK7/DJ1 protein in both lanes.
This product has been referenced in:
- Gao L et al. Natrium Benzoate Alleviates Neuronal Apoptosis via the DJ-1-Related Anti-oxidative Stress Pathway Involving Akt Phosphorylation in a Rat Model of Traumatic Spinal Cord Injury. Front Mol Neurosci 12:42 (2019). Read more (PubMed: 30853891) »
- Jang J et al. Oxidized DJ-1 Levels in Urine Samples as a Putative Biomarker for Parkinson's Disease. Parkinsons Dis 2018:1241757 (2018). Read more (PubMed: 29887985) »