Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

PARK7

Uniprot No.

Q99497

Research Area

Cancer

Alternative Names

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

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

1-188aa

Target Protein Sequence

MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVLK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

19.8 kDa

Protein Length

Partial

Tag Info

Tag-Free

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

Discover the potential of Recombinant Human Parkinson Disease Protein 7 (PARK7) in cancer research with our premium quality product. PARK7, also known as DJ-1, has been implicated in various cellular processes, including oxidative stress response, cell survival, and transcriptional regulation. Its multifaceted role in cancer progression and response to therapies makes it an intriguing target for researchers in the field.

Our Recombinant Human PARK7 protein is expressed in an E.coli system, ensuring a reliable and high-quality source of protein for your research needs. The partial protein sequence (1-188aa) is delivered in a tag-free format, providing an unmodified protein that closely mimics its native form. Boasting a purity greater than 90% as determined by SDS-PAGE, our PARK7 protein ensures consistent and reproducible results across various applications. Available in both liquid and lyophilized powder forms, our Recombinant Human PARK7 protein is tailored to meet the diverse requirements of your cancer research endeavors.

Target Background

Function

Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease. 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. Has been described as a 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. But this function is rebuted by other works. As a protein deglycase, 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. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels. Displays a very low glyoxalase activity that may reflect its deglycase activity. 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.

Gene References into Functions

DJ-1 protein concentration was significantly increased during the clinical phase in cerebrospinal fluid of sporadic Creutzfeldt-Jakob disease patients. PMID: 27975168
The Parkinsonism-associated protein DJ-1 and its bacterial homologs deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL function as deglycases that repair proteins and nucleotides from endogeneous glycation by glyoxal and methylglyoxal. DJ-1, deglycase 1 and deglycase 2 repair glyoxal- and methylglyoxal-glycated substrates, whereas deglycase 3 principally repairs glyoxal-glycated substrates. PMID: 29932913
Data of this study showed that DJ-1 downregulation increased apoptosis and reduced migration by regulating matrix metalloproteinase 2 and matrix metalloproteinase 9 in HTR-8/SVneo cells under both ambient and oxidative stress. PMID: 29258409
NRF2, DJ1 and SRNX1 are commonly expressed in diffusely infiltrating astrocytomas and they can be used in predicting patient prognosis. PMID: 29441509
Low PARK7 expression is associated with pre-term birth. PMID: 29358306
The results suggest that the impaired mitochondrial activity could be due to the broken interaction between DJ-1 and NDUFS3 and that downregulation of DJ-1 in sperm and testes contributes to AS pathogenesis. PMID: 29849492
In this review, we discuss the role as well as the underlying molecular mechanisms of DJ-1 in ocular diseases, including Fuchs endothelial corneal dystrophy (FECD), age-related macular degeneration (AMD), cataracts, and ocular neurodegenerative diseases, highlighting that DJ-1 may serve as a very striking therapeutic target for ocular diseases. PMID: 29559831
Novel candidate genes of the PARK7 interactome play a role in MS. PMID: 29100048
results indicated that oxDJ-1 levels in erythrocytes can be used as a marker for the differential diagnosis of Parkinson's disease PMID: 28705587
DJ-1 promoter polymorphism is associated with male infertility. PMID: 28932933
The PD-associated L166P mutant, but not wild-type DJ-1, directly binds to and is cleaved by the mitochondrial serine protease Omi at both serine residues 3 and 121. PMID: 29177768
DJ-1 plays a major role in various signaling pathways. Related to its anti-oxidant properties, it mediates cell survival and proliferation by activating the extracellular signal-regulated kinase (ERK1/2) pathway and attenuates cell death signaling by inhibiting apoptosis signal-regulating kinase 1 (ASK1) activation. [review] PMID: 28954246
the present study highlighted the involvement of DJ1 in HGrelated EC injury and identified that DJ1 exerts a cellular protective effect in HUVECs exposed to HG induced oxidative stress via activation of the PI3K/AkteNOS signaling pathway. PMID: 29115508
These findings suggest that oxidation-induced ubiquitination and degradation can be a quality control mechanism of oxidized redox-sensitive proteins including Prxs and DJ-1. PMID: 27703196
study implies that DJ-1 may protect endothelial progenitor cells against Ang II-induced dysfunction by activating the PPARgamma/HO-1. PMID: 28600848
Study shows the generation of oxDJ-1 in erythrocytes in early stage, unmedicated parkinson's disease (PD) patients and in non-human primates with PD symptoms. In addition, oxDJ-1 interacts with 20S proteasome in the erythrocytes of PD patients. The current findings suggest that oxidative stress is systemically present in PD patients and suggest that an early pathophysiological mechanism operates in PD. PMID: 27470541
Not only is protein deglycase DJ-1 (DJ-1) linked to familial Parkinson's disease (PD), but it is also associated with the pathogenic mechanisms of sporadic PD and other neurodegenerative disorders where oxidative stress is implicated [Review]. PMID: 29147901
Studies indicate that protein deglycase DJ-1 (DJ-1) plays a critical role in cancer [Review] PMID: 29147902
Studies indicate that sperm protein deglycase DJ-1 (DJ-1 concentration in Asthenozoospermia is lower than that in control. PMID: 29147903
Studies indicate Cys-106-oxidized protein deglycase DJ-1(oxDJ-1) levels in the brain and blood as a biomarker candidate for early-phase Parkinson's disease. PMID: 29147908
Data suggest that protein deglycase DJ-1 (DJ-1) plays multiple roles in many cell types under metabolically challenging conditions as seen in obesity, insulin resistance, and type 2 diabetes mellitus [Review]. PMID: 29147909
Studies suggest that protein deglycase DJ-1 (DJ-1) plays a critical role in tumor development and progression, and also as a therapeutic target against cancer. PMID: 29147911
The clinical pattern of multisystem involvement and the biochemical findings in our patient highlight the role for DJ-1 in modulating mitochondrial response against oxidative stress. PMID: 27460976
Oxidised DJ-1 was significantly decreased in idiopathic PD brain, suggesting altered complex function may also play a role in the more common sporadic form of the disease. PMID: 29016861
High DJ1 expression is associated with breast cancer. PMID: 27582551
Three types of pathogenic mutants of DJ-1 (M26I, D149A and L166P) have been reported to disrupt proper structures and lead to a loss of function--{REVIEW} PMID: 28458339
the results suggest that over-oxidation may trigger loss of functions due to local structural modification in the Cys106 containing pocket of DJ-1 and structurally destabilize the dimeric state of DJ-1, which is believed to be its bioactive conformation. Such loss of functions would result in reduced ability of DJ-1 to protect from oxidative stress insults and may lead to increased progression of disease. PMID: 28844983
This study demonstrated that the DJ1 mutations account for approximately 5% of EOPD patients from the Indian population. PMID: 27592010
This report describe a new homozygous c.133C > T transition in DJ1 segregating with PD and ALS in a family from eastern Turkey. PMID: 26972524
SiRNA-mediated DJ-1 knockdown reduced myeloma cell growth under a hypoxic microenvironment. PMID: 27734217
chaperone-mediated autophagy protects mitochondrial function by degrading nonfunctional PARK7 and maintaining its homeostasis, and dysregulation of this pathway may contribute to the neuronal stress and death in Parkinson disease pathogenesis PMID: 27171370
DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system named guanine glycation repair. PMID: 28596309
Taken together, our results provide a structural basis for the binding mechanism between DJ-1 and Bcl-XL, which will contribute to molecular understanding of the role of mitochondrial DJ-1 in Bcl-XL regulation in response to oxidative stress. PMID: 29175327
Results suggest that overexpression of DJ-1 improves mitochondrial function, at least in part, through a mechanism involving Akt phosphorylation on threonine 308. PMID: 26913805
Hsp31 is a homodimeric protein structurally similar to human DJ-1, a Parkinson's disease-linked protein, and both are members of the DJ-1/ThiJ/PfpI superfamily. PMID: 27097320
DJ-1 co-aggregating with alpha-synuclein may result from weak hydrophobic interaction and DJ-1 exhibited chaperon-like activity in the initial time of alpha-synuclein aggregation at high temperature. PMID: 28330770
The effects of variants in the Parkin, PINK1, and DJ-1 genes along with evidence for their pathogenicity have been summarized. (Review) PMID: 26965687
genetic analyses of indel loci in ACE, DJ-1, and GIGYF2 genes, was performed to explore the potential contribution of insertion (I)/deletion (D) polymorphisms (indels) to the risk of PD in a Chinese population. PMID: 28873462
DJ-1 deficiency negatively regulates liver progenitor cells (LPC) proliferation by impairing the formation of LPC-associated fibrosis and inflammatory niches. PMID: 27277679
Downregulation of DJ-1 using DJ-1-siRNA in H69AR cells sensitized cancer cells to chemotherapeutic drugs through increasing drug-induced cell apoptosis accompanied with G0-G1 phase arrest. These findings suggest DJ-1 may serve as a potential biomarker for chemoresistance and prognostic factor for patients with small-cell lung cancer (SCLC). PMID: 28580701
regulation of reactive oxygen species (ROS) and of the antioxidant protein DJ-1 (PARK-7), which increases with cancer progression and acts to lessen oxidative damage to malignant cells, in relationship with systemic mastocytosis severity, was examined. PMID: 27611333
DJ-1 was highly expressed in the early stage of lung cancer, and its expression was significantly decreased after metastasis. Therefore, DJ-1 may be a potential biomarker for the early diagnosis and monitoring of lung cancer metastasis PMID: 28653888
DJ-1 overexpression can restore the impaired Nrf2 pathway, leading to Alveolar type II cell protection in heavy smokers. PMID: 27093578
DJ-1 serum levels seem to be correlated with worsening of the endometrial cancer grade and histotype, making it a reliable tool in the preoperative decision-making process. PMID: 28618925
DJ-1 family deglycases repair proteins from glycation by glyoxals. Contradictory results suggested that this activity resulted from a Tris artefact. We show here that DJ-1 behaves indeed as a bona fide deglycase. PMID: 28013050
ELISA-based detection of flotillin 2 and PARK7 showed that the combination of these proteins was able to distinguish prostate cancer patients and healthy controls with 68% sensitivity and 93% specificity PMID: 27664330
Furthermore, SIRT1 activity was reduced in DJ-1-knockout cells, and this reduced activity was restored by re-introduction of wild-type DJ-1 but not of C106-mutant DJ-1 into DJ-1-knockout cells. It is first report showing direct connection of DJ-1 with SIRT1. PMID: 27105916
DJ-1 is necessary for 20C-mediated protection against rotenone-induced oxidative damage, at least in part, by activating PI3K/Akt signaling, and subsequently enhancing the nuclear accumulation of Nrf2. PMID: 28245986
The aberrant up-regulation of DJ-1 expression might be an important step in the pathogenesis of cervical carcinoma. PMID: 27544688
Association of early onset Parkinson' and severe clinical signs with multiple alterations in DJ1 in Turkish patients. PMID: 27455133

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Involvement in disease

Parkinson disease 7 (PARK7)

Subcellular Location

Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion. Endoplasmic reticulum.

Protein Families

Peptidase C56 family

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 panc

Database Links

HGNC: 16369

OMIM: 168600

KEGG: hsa:11315

STRING: 9606.ENSP00000340278

UniGene: Hs.419640

Code	CSB-EP860342HU1e1
Abbreviation	Recombinant Human PARK7 protein, partial
MSDS	MSDS Datasheet
Size	$390
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Parkinson disease protein 7 (PARK7), partial

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