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PARK2 recombinant protein :: E3 ubiquitin-protein ligase parkin Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS1070644
SDS-PAGE
Unit / Price
0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
0.01 mg (Baculovirus)  /  $120 +1 FREE 8GB USB
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
0.05 mg (Yeast)  /  $975 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
0.2 mg (Yeast)  /  $1,310 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,350 +1 FREE 8GB USB
0.5 mg (Yeast)  /  $1,485 +1 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $2,035 +2 FREE 8GB USB
1 mg (Yeast)  /  $2,255 +2 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

E3 ubiquitin-protein ligase parkin (PARK2), Recombinant Protein

★Popular Item★
 Also Known As   

Recombinant Human E3 ubiquitin-protein ligase parkin

 Product Synonym Names    Parkinson juvenile disease protein 2; Parkinson disease protein 2
 Product Gene Name   

PARK2 recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 MBS1070644 COA    COA PDF
 Sequence Positions    1-465aa; Full Length
 Sequence    MIVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL RNDWTVQNCD LDQQSIVHIV QRPWRKGQEM NATGGDDPRN AAGGCEREPQ SLTRVDLSSS VLPGDSVGLA VILHTDSRKD SPPAGSPAGR SIYNSFYVYC KGPCQRVQPG KLRVQCSTCR QATLTLTQGP SCWDDVLIPN RMSGECQSPH CPGTSAEFFF KCGAHPTSDK ETSVALHLIA TNSRNITCIT CTDVRSPVLV FQCNSRHVIC LDCFHLYCVT RLNDRQFVHD PQLGYSLPCV AGCPNSLIKE LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEPDQRKV TCEGGNGLGC GFAFCRECKE AYHEGECSAV FEASGTTTQA YRVDERAAEQ ARWEAASKET IKKTTKPCPR CHVPVEKNGG CMHMKCPQPQ CRLEWCWNCG CEWNRVCMGD HWFDV
 OMIM    168600
 3D Structure    ModBase 3D Structure for O60260
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal Myc-tag. N-terminal host tags may vary (His, His-SUMO, His-B2M, GST). Tag types are determined by various factors including tag-protein stability and, therefore, are subject to change; please inquire for tag information.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of PARK2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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Product Description specifically for PARK2 recombinant protein

   Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the roval and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30. Preferentially assbles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy. Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene
 Product Categories/Family for PARK2 recombinant protein    Apoptosis
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 SDS-PAGE of PARK2 recombinant protein    PARK2 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for PARK2. It may not necessarily be applicable to this product.
 NCBI GI #    169790969
 NCBI GeneID    5071
 NCBI Accession #    NP_004553.2 [Other Products]
 NCBI GenBank Nucleotide #    NM_004562.2 [Other Products]
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 UniProt Primary Accession #    O60260 [Other Products]
 UniProt Secondary Accession #    Q5TFV8; Q5VVX4; Q6Q2I6; Q8NI41; Q8NI43; Q8NI44; Q8WW07; A3FG77; A8K975; D3JZW7; D3K2X0 [Other Products]
 UniProt Related Accession #    O60260 [Other Products]
 Molecular Weight    67.6kD
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 NCBI Official Full Name    E3 ubiquitin-protein ligase parkin isoform 1
 NCBI Official Synonym Full Names    parkin RBR E3 ubiquitin protein ligase
 NCBI Official Symbol    PARK2 [Similar Products]
 NCBI Official Synonym Symbols   
PDJ; PRKN; AR-JP; LPRS2
[Similar Products]
 NCBI Protein Information    E3 ubiquitin-protein ligase parkin
 UniProt Protein Name    E3 ubiquitin-protein ligase parkin
 UniProt Synonym Protein Names   
Parkinson juvenile disease protein 2; Parkinson disease protein 2
 Protein Family    E3 ubiquitin-protein ligase
 UniProt Gene Name    PARK2 [Similar Products]
 UniProt Synonym Gene Names    PRKN; Parkin; Parkinson disease protein 2 [Similar Products]
 UniProt Entry Name    PRKN2_HUMAN
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 NCBI Summary for PARK2    The precise function of this gene is unknown; however, the encoded protein is a component of a multiprotein E3 ubiquitin ligase complex that mediates the targeting of substrate proteins for proteasomal degradation. Mutations in this gene are known to cause Parkinson disease and autosomal recessive juvenile Parkinson disease. Alternative splicing of this gene produces multiple transcript variants encoding distinct isoforms. Additional splice variants of this gene have been described but currently lack transcript support. [provided by RefSeq, Jul 2008]
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 UniProt Comments for PARK2    PARK2: a component of a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'- linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria. Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in role in regulation of neuron death. Limits the production of reactive oxygen species (ROS). Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin-E during neuronal apoptosis. May represent a tumor suppressor gene. Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1. Part of a SCF-like complex, consisting of PARK2, CUL1 and FBXW7. Part of a complex, including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PARK2 and GPR37, thus facilitating PARK2-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PARK2, whereas, STUB1 enhances the E3 activity of PARK2 through promotion of dissociation of HSP70 from PARK2-GPR37 complexes. Interacts with PSMD4 and PACRG. Interacts with LRRK2. Interacts with RANBP2. Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination. Interacts (via first RING- type domain) with AIMP2 (via N-terminus). Interacts with PSMA7 and RNF41. Interacts with PINK1. Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis. Found in serum. Belongs to the RBR family. Parkin subfamily. 6 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 6.3.2.-; EC 6.3.2.19; Ligase; Ubiquitin conjugating system; Ubiquitin ligase

Chromosomal Location of Human Ortholog: 6q25.2-q27

Cellular Component: cytoplasm; cytosol; endoplasmic reticulum; Golgi apparatus; mitochondrion; neuron projection; nucleus; perinuclear region of cytoplasm; SCF ubiquitin ligase complex; ubiquitin ligase complex

Molecular Function: actin binding; beta-catenin binding; chaperone binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; histone deacetylase binding; Hsp70 protein binding; identical protein binding; kinase binding; PDZ domain binding; phospholipase binding; protein binding; protein kinase binding; SH3 domain binding; transcription factor activity; tubulin binding; ubiquitin binding; ubiquitin conjugating enzyme binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; zinc ion binding

Biological Process: adult locomotory behavior; cellular protein catabolic process; cellular protein metabolic process; central nervous system development; dopamine metabolic process; macroautophagy; mitochondrial fission; mitochondrion degradation; mitochondrion organization and biogenesis; negative regulation of actin filament bundle formation; negative regulation of glucokinase activity; negative regulation of insulin secretion; negative regulation of JNK cascade; negative regulation of neuron apoptosis; negative regulation of protein amino acid phosphorylation; negative regulation of transcription from RNA polymerase II promoter; positive regulation of DNA binding; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of neurotransmitter uptake; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of protein binding; positive regulation of protein catabolic process; positive regulation of transcription from RNA polymerase II promoter; proteasomal protein catabolic process; proteasomal ubiquitin-dependent protein catabolic process; protein autoubiquitination; protein destabilization; protein monoubiquitination; protein polyubiquitination; protein stabilization; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of autophagy; regulation of dopamine metabolic process; regulation of dopamine secretion; regulation of lipid transport; regulation of protein stability; regulation of protein ubiquitination; response to oxidative stress; zinc ion homeostasis

Disease: Leprosy, Susceptibility To, 2; Lung Cancer; Ovarian Cancer; Parkinson Disease 2, Autosomal Recessive Juvenile
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Product References and Citations for PARK2 recombinant protein

   Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism.Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., Shimizu N.Nature 392:605-608(1998) Evidence for the presence of full-length PARK2 mRNA and Parkin protein in human blood.Kasap M., Akpinar G., Sazci A., Idrisoglu H.A., Vahaboglu H.Neurosci. Lett. 460:196-200(2009) Functional and molecular diversity of parkin.D'Agata V., Scapagnini G., Cavallaro S.Homo sapiens PARK2 transcript variants.Campello L., Esteve-Rudd J., Cuenca N., Martin-Nieto J. 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 analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003)
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 Research Articles on PARK2    1. suggests that a novel binding mechanism between Parkin and ubiquitin leads to a Parkin conformational change with subsequent activation of Parkin E3 ligase activity
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with PARK2 recombinant proteinPathways associated with PARK2 recombinant protein
 Reference Product  PubMed Publications
 PINK1 recombinant protein  >612 publications with PARK2 and PINK1
 UBC recombinant protein  >100 publications with PARK2 and UBC
 SNCAIP recombinant protein  >64 publications with PARK2 and SNCAIP
 GPR37 recombinant protein  >23 publications with PARK2 and GPR37
 UBE2L3 recombinant protein  >10 publications with PARK2 and UBE2L3
 PSMD4 recombinant protein  >3 publications with PARK2 and PSMD4
 UBE2N recombinant protein  >2 publications with PARK2 and UBE2N
 UBE2G1 recombinant protein  >1 publications with PARK2 and UBE2G1
 Products by Pathway  Pathway Diagram
 Adaptive Immune System Pathway antibodies  Adaptive Immune System Pathway Diagram
 Alpha-synuclein Signaling Pathway antibodies  Alpha-synuclein Signaling Pathway Diagram
 Amyloid Fiber Formation Pathway antibodies  Amyloid Fiber Formation Pathway Diagram
 Antigen Processing: Ubiquitination & Proteasome Degradation Pathway antibodies  Antigen Processing: Ubiquitination & Proteasome Degradation Pathway Diagram
 Class I MHC Mediated Antigen Processing & Presentation Pathway antibodies  Class I MHC Mediated Antigen Processing & Presentation Pathway Diagram
 Immune System Pathway antibodies  Immune System Pathway Diagram
 Metabolism Of Proteins Pathway antibodies  Metabolism Of Proteins Pathway Diagram
 Mitophagy Pathway antibodies  Mitophagy Pathway Diagram
 Parkin-Ubiquitin Proteasomal System Pathway antibodies  Parkin-Ubiquitin Proteasomal System Pathway Diagram
 Parkinson's Disease Pathway antibodies  Parkinson's Disease Pathway Diagram
Diseases associated with PARK2 recombinant proteinOrgans/Tissues associated with PARK2 recombinant protein
 Disease Name  Pubmed Publications
 Parkinsonian Disorders Antibodies  >62960 publications with PARK2 and Parkinsonian Disorders
 Nervous System Diseases Antibodies  >62650 publications with PARK2 and Nervous System Diseases
 Movement Disorders Antibodies  >62616 publications with PARK2 and Movement Disorders
 Brain Diseases Antibodies  >62505 publications with PARK2 and Brain Diseases
 Parkinson Disease Antibodies  >55679 publications with PARK2 and Parkinson Disease
 Neurodegenerative Diseases Antibodies  >53992 publications with PARK2 and Neurodegenerative Diseases
 Parkinson Disease, Secondary Antibodies  >6812 publications with PARK2 and Parkinson Disease, Secondary
 Disease Models, Animal Antibodies  >5328 publications with PARK2 and Disease Models, Animal
 Cognition Disorders Antibodies  >3762 publications with PARK2 and Cognition Disorders
 Neurotoxicity Syndromes Antibodies  >3535 publications with PARK2 and Neurotoxicity Syndromes
 Organ/Tissue Name  Pubmed Publications
 Brain Antibodies  >27744 publications with PARK2 and Brain
 Eye Antibodies  >1163 publications with PARK2 and Eye
 Adrenal Gland Antibodies  >442 publications with PARK2 and Adrenal Gland
 Mouth Antibodies  >291 publications with PARK2 and Mouth
 Kidney Antibodies  >216 publications with PARK2 and Kidney
 Stomach Antibodies  >106 publications with PARK2 and Stomach
 Connective Tissue Antibodies  >61 publications with PARK2 and Connective Tissue
 Prostate Antibodies  >47 publications with PARK2 and Prostate
 Testis Antibodies  >25 publications with PARK2 and Testis
 Placenta Antibodies  >11 publications with PARK2 and Placenta
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