Recombinant Human Parkinson Disease Protein 7 (PARK7) Protein (His-GST)

Name: Recombinant Human Parkinson Disease Protein 7 (PARK7) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-07973P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Parkinson Disease Protein 7 (PARK7) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Uniprotkb	Q99497
Target Symbol	PARK7
Synonyms	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)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNG
Expression Range	1-174aa
Protein Length	Partial
Mol. Weight	48.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion. Endoplasmic reticulum.
Protein Families	Peptidase C56 family
Database References	HGNC: 16369 OMIM: 168600 KEGG: hsa:11315 STRING: 9606.ENSP00000340278 UniGene: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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