PARK7 ELISA Kit (Rat) (OKCA01920)

OKCA01920

PARK7 ELISA Kit (Rat) (OKCA01920)

Description of target: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines 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). 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. Its involvement in protein repair could also explain other unrelated functions. 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. 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.;Species reactivity: Rat;Application: ;Assay info: Assay Methodology: Quantitative Sanadwich ELISA;Sensitivity: 0.078 ng/mL

1679.8 €

OKCA01920-96W

OKCA01920-96W - PARK7 ELISA Kit (Rat)

1207 €

ELI-14714r

Park7/ Rat Park7 ELISA Kit

1475.84 €

OKCD00717

PARK7 ELISA Kit (Human) (OKCD00717)

Description of target: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines 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) (PubMed:25416785). 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 (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785). 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 (PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745). Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:19229105, PubMed:16632486). 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 (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957).By similarity&#xd; &lt;p>Manually curated information which has been propagated from a related experimentally characterized protein.&lt;/p>&#xd; &#xd; &#xd; &lt;p>&lt;a href="/manual/evidences#ECO:0000250">More…&lt;/a>&lt;/p> Manual assertion inferred from sequence similarity toiUniProtKB:Q99LX0&nbsp;(PARK7_MOUSE)21 Publications&#xd; &lt;p>Manually curated information for which there is published experimental evidence.&lt;/p>&#xd; &#xd; &#xd; &lt;p>&lt;a href="/manual/evidences#ECO:0000269">More…&lt;/a>&lt;/p> Manual assertion based on experiment iniRef.1"DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras."_x005F_x005F_x000D_Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H._x005F_x005F_x000D_Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.Ref.11"DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."_x005F_x005F_x000D_Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H._x005F_x005F_x000D_J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.Ref.14"DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."_x005F_x005F_x000D_Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H._x005F_x005F_x000D_Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EFCAB6, COMPONENT OF A COMPLEX COMPOSED OF AR; EFCAB6 AND PARK7.Ref.18"DJ-1 has a role in antioxidative stress to prevent cell death."_x005F_x005F_x000D_Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H._x005F_x005F_x000D_EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF VAL-51 AND CYS-53.Ref.19"DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."_x005F_x005F_x000D_Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A._x005F_x005F_x000D_PLoS Biol. 2:1-10(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.Ref.21"Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."_x005F_x005F_x000D_Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H._x005F_x005F_x000D_Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.Ref.22"DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."_x005F_x005F_x000D_Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H._x005F_x005F_x000D_Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-106.Ref.23"DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."_x005F_x005F_x000D_Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.24"RNA binding activity of the recessive parkinsonism protein DJ-1 supports involvement in multiple cellular pathways."_x005F_x005F_x000D_van der Brug M.P., Blackinton J., Chandran J., Hao L.Y., Lal A., Mazan-Mamczarz K., Martindale J., Xie C., Ahmad R., Thomas K.J., Beilina A., Gibbs J.R., Ding J., Myers A.J., Zhan M., Cai H., Bonini N.M., Gorospe M., Cookson M.R._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 105:10244-10249(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.25"Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation."_x005F_x005F_x000D_Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K., Jiang W., Ronai Z., Zhuang X., Zhang Z._x005F_x005F_x000D_J. Clin. Invest. 119:650-660(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COMPONENT OF A COMPLEX COMPOSED OF PARK2; PARK7 AND PINK1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK7 PRO-166.Ref.26"Mitochondrial localization of DJ-1 leads to enhanced neuroprotection."_x005F_x005F_x000D_Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M._x005F_x005F_x000D_J. Neurosci. Res. 87:123-129(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.Ref.27"Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."_x005F_x005F_x000D_Chen J., Li L., Chin L.S._x005F_x005F_x000D_Hum. Mol. Genet. 19:2395-2408(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, MUTAGENESIS OF CYS-106 AND HIS-126.Ref.29"DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."_x005F_x005F_x000D_McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P._x005F_x005F_x000D_J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, MUTAGENESIS OF CYS-106.Ref.30"Human DJ-1 and its homologs are novel glyoxalases."_x005F_x005F_x000D_Lee J.Y., Song J., Kwon K., Jang S., Kim C., Baek K., Kim J., Park C._x005F_x005F_x000D_Hum. Mol. Genet. 21:3215-3225(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CAUTION, MUTAGENESIS OF GLU-18; CYS-106 AND HIS-126, CHARACTERIZATION OF VARIANT PARK7 PRO-166.Ref.31"DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."_x005F_x005F_x000D_Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M._x005F_x005F_x000D_Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46 AND CYS-106, CHARACTERIZATION OF VARIANT PARK7 PRO-166.Ref.32"Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity."_x005F_x005F_x000D_Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M., Xu X.M., Brede C., Larsen J.P., Moller S.G._x005F_x005F_x000D_J. Biol. Chem. 288:22809-22820(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COPPER-BINDING, CHARACTERIZATION OF VARIANTS PARK7 THR-104 AND ALA-149, MUTAGENESIS OF CYS-106.Ref.34"Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine and lysine residues."_x005F_x005F_x000D_Richarme G., Mihoub M., Dairou J., Bui L.C., Leger T., Lamouri A._x005F_x005F_x000D_J. Biol. Chem. 290:1885-1897(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CAUTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, COFACTOR.Ref.39"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."_x005F_x005F_x000D_Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S._x005F_x005F_x000D_J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106, HOMODIMERIZATION.Ref.40"The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."_x005F_x005F_x000D_Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, LACK OF PROTEOLYTIC ACTIVITY.Ref.41"The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization."_x005F_x005F_x000D_Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.Ref.52"Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."_x005F_x005F_x000D_Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R._x005F_x005F_x000D_PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ASP-64, FUNCTION. ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.60 ng/mL

1793.2 €

OKCD09272

PARK7 ELISA Kit (Mouse) (OKCD09272)

Description of target: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines 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). 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 and cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Its involvement in protein repair could explain other unrelated functions. 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. 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.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: < 0.059ng/mL

1841.8 €

EF019140

Park7 ELISA Kit| Rat Protein deglycase DJ-1 ELISA Kit

1192.16 €