protein

Recombinant Human Protein DJ-1

MBS717208

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Protein DJ-1

DJ-1

Oncogene DJ1; Parkinson disease protein 7

protein DJ-1; Protein deglycase DJ-1; protein deglycase DJ-1; Parkinsonism associated deglycase; Oncogene DJ1; Parkinson disease protein 7

PARK7

DJ-1

PARK7; PARK7; DJ1; DJ-1; HEL-S-67p; DJ-1

PARK7_HUMAN

E Coli

1-188

189

MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLA
GKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLG
AQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEI
GFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSR
GPGTSFEFALAIVEALNGKEVAAQVKAPLVLK

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Apoptosis

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 (hithioacetals 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 involvent 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 pacaking. 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.

DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras.Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.Biochem. Biophys. Res. Commun. 231:509-513(1997) Homo sapiens RNA-binding protein regulatory subunit mRNA.Beaudoin R., Hod Y. Human DJ-1 cDNA from PC3 cells.Ariga H., Niki T.Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

183227678

NP_001116849.1

NM_001123377.1

Q99497

47.2kD

Alpha-synuclein Signaling Pathway (137913); Androgen Receptor Signaling Pathway (198806); Parkinson's Disease Pathway (83098); Parkinsons Disease Pathway (705377); Synaptic Vesicle Pathway (672457)

The product of this gene belongs to the peptidase C56 family of proteins. It acts as a positive regulator of androgen receptor-dependent transcription. It may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death. Defects in this gene are the cause of autosomal recessive early-onset Parkinson disease 7. Two transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008]

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. Protein type: EC 3.4.-.-; Nuclear receptor co-regulator; Transcription regulation; Tumor suppressor. Chromosomal Location of Human Ortholog: 1p36.23. Cellular Component: axon; chromatin; cytoplasm; cytosol; endoplasmic reticulum; lipid raft; mitochondrial intermembrane space; mitochondrial matrix; mitochondrial respiratory chain complex I; mitochondrion; nucleus; plasma membrane; PML body. Molecular Function: androgen receptor binding; copper ion binding; cytokine binding; double-stranded DNA binding; enzyme binding; glyoxalase III activity; identical protein binding; kinase binding; mercury ion binding; mRNA binding; oxidoreductase activity, acting on peroxide as acceptor; peptidase activity; peroxiredoxin activity; protein binding; protein homodimerization activity; receptor binding; single-stranded DNA binding; superoxide dismutase copper chaperone activity; transcription coactivator activity; transcription factor binding. Biological Process: activation of protein kinase B; adult locomotory behavior; autophagy; detoxification of copper ion; detoxification of mercury ion; dopamine uptake; enzyme active site formation via L-cysteine sulfinic acid; glycolate biosynthetic process; hydrogen peroxide metabolic process; inflammatory response; lactate biosynthetic process; membrane depolarization; membrane hyperpolarization; methylglyoxal catabolic process to D-lactate; mitochondrion organization and biogenesis; negative regulation of apoptosis; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of protein amino acid phosphorylation; negative regulation of protein binding; negative regulation of protein export from nucleus; negative regulation of protein kinase activity; negative regulation of protein sumoylation; negative regulation of protein ubiquitination; negative regulation of ubiquitin-protein ligase activity; positive regulation of interleukin-8 production; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; protein deglycosylation; protein stabilization; proteolysis; Ras protein signal transduction; regulation of inflammatory response; regulation of mitochondrial membrane potential; regulation of neuron apoptosis; regulation of TRAIL receptor biosynthetic process; response to drug; single fertilization. Disease: Parkinson Disease 7, Autosomal Recessive Early-onset

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180