Product: PARK7 Antibody
Catalog: AF0380
Description: Rabbit polyclonal antibody to PARK7
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 20kDa,26kDa; 20kD(Calculated).
Uniprot: Q99497
RRID: AB_2833539

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

WB 1:500-1:3000, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Zebrafish(100%), Bovine(88%), Horse(88%), Sheep(88%), Rabbit(88%), Dog(88%), Chicken(88%)
PARK7 Antibody detects endogenous levels of total PARK7.
Cite Format: Affinity Biosciences Cat# AF0380, RRID:AB_2833539.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


CAP1; DJ-1; DJ1; DJ1 protein; Epididymis secretory sperm binding protein Li 67p; FLJ27376; FLJ34360; FLJ92274; HEL S 67p; Oncogene DJ1; OTTHUMP00000001348; OTTHUMP00000001349; OTTHUMP00000001350; OTTHUMP00000001351; PARK7; PARK7_HUMAN; Parkinson disease (autosomal recessive, early onset) 7; Parkinson disease protein 7; Parkinson protein 7; Protein DJ-1; SP22;



Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. Expressed by pancreatic islets at higher levels than surrounding exocrine tissues (PubMed:22611253).

DJ-1 associated with autosomal recessive early onset parkinsonism. Involved in the oxidative stress response. Three cysteines in DJ-1 may be oxidized to cysteine sulphonic acid in the cellular response to H2O2. Loss of DJ-1 function may lead to neurodegeneration.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q99497 As Substrate

Site PTM Type Enzyme
A2 Acetylation
T19 Phosphorylation
R27 Methylation
K32 Ubiquitination
K41 Acetylation
K41 Ubiquitination
C46 S-Nitrosylation
S47 Phosphorylation
C53 S-Nitrosylation
S57 Phosphorylation
K62 Acetylation
K62 Ubiquitination
K63 Acetylation
K63 Ubiquitination
Y67 Phosphorylation
K89 Ubiquitination
K93 Ubiquitination
K99 Ubiquitination
K130 Acetylation
K130 Sumoylation
K130 Ubiquitination
K132 Acetylation
Y139 Phosphorylation
Y141 Phosphorylation
S142 Phosphorylation
K148 Acetylation
K148 Ubiquitination
T154 Phosphorylation
K175 Ubiquitination
K182 Ubiquitination
K188 Ubiquitination

Research Backgrounds


Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. 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. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity. In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity).


Sumoylated 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.

Subcellular Location:

Cell membrane>Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion. Endoplasmic reticulum.
Note: 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 (PubMed:18711745). Detected in tau inclusions in brains from neurodegenerative disease patients (PubMed:14705119). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. Expressed by pancreatic islets at higher levels than surrounding exocrine tissues.

Subunit Structure:

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF. Forms a complex with PINK1 and PRKN. Interacts (via C-terminus) with NCF1; the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (By similarity). Interacts with NENF.


Belongs to the peptidase C56 family.

Research Fields

· Human Diseases > Neurodegenerative diseases > Parkinson's disease.

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