Anti-PARK7 antibody

Rabbit polyclonal against PARK7

Product Information

Model STJ94957
Host Rabbit
Reactivity Human, Mouse
Applications ELISA, IF, IHC-p, WB
Immunogen Synthesized peptide derived from human PARK7
Gene ID 11315
Dilution range WB 1:500-1:2000
IHC 1:100-1:300
IF 1:200-1:1000
ELISA 1:10000
Specificity PARK7 polyclonal antibody detects endogenous levels of PARK7 protein.
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Protein Name Protein/Nucleic Acid Deglycase Dj-1
Maillard Deglycase
Oncogene Dj1
Parkinson Disease Protein 7
Parkinsonism-Associated Deglycase
Protein Dj-1
Clonality Polyclonal
Conjugation Unconjugated
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Concentration 1 mg/ml
Storage Instruction Store at-20°C, and avoid repeat freeze-thaw cycles.
Database Links HGNC:16369
Alternative Names Anti-Protein/Nucleic Acid Deglycase Dj-1 antibody
Anti-Maillard Deglycase antibody
Anti-Oncogene Dj1 antibody
Anti-Parkinson Disease Protein 7 antibody
Anti-Parkinsonism-Associated Deglycase antibody
Anti-Protein Dj-1 antibody
Anti-Dj-1 antibody
Anti-PARK7 antibody
Function 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. 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.
Cellular Localization Cell Membrane
Membrane Raft
Endoplasmic Reticulum
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
Membrane Raft Localization In Astrocytes And Neuronal Cells Requires Palmitoylation
Post-translational Modifications 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.

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