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MAB5512 Anti-Parkin Antibody, clone PRK8

100 µL  
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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, MIP, WB, IHCMAscitesMonoclonal Antibody
      Catalogue NumberMAB5512
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Parkin Antibody, clone PRK8
      Product Information
      PresentationAscites fluid. Liquid. Contains no preservative.
      Quality LevelMQ100
      ApplicationAnti-Parkin Antibody, clone PRK8 is an antibody against Parkin for use in IP, WB, IH.
      Key Applications
      • Immunoprecipitation
      • Western Blotting
      • Immunohistochemistry
      Application NotesWestern blot. The antibody detects ~50 and ~44 kDa bands in mouse brain extracts. In human brain extracts the antibody reacts with ~50 and ~46 kDa. Immunohistochemistry



      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenRecombinant human parkin.
      SpecificityParkin. The epitope recognizes by the monoclonal is between animo acids 399-465 of human parkin. The antibody shows no cross-reactivity with protein in extracts from parkin null mice.
      Species Reactivity
      • Human
      • Mouse
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThe 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.
      Gene Symbol
      • PARK2
      • PDJ
      • PRKN
      • LPRS2
      • AR-JP
      • parkin
      • EC 6.3.2.-
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: O60260 # Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. 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.
      SIZE: 465 amino acids; 51641 Da
      SUBUNIT: Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Part of a SCF-like complex, consisting of PARK2, CUL1 and FBXW7. Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11. Interacts and regulates the turnover of SEPT5. 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.
      SUBCELLULAR LOCATION: Cytoplasm. Note=Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. Nucleus.
      TISSUE SPECIFICITY: 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.
      DOMAIN: SwissProt: O60260 The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes.
      PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. & S-nitrosylated. The inhibition of PARK2 ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in PD by impairing the ubiquitination of PARK2 substrates.
      DISEASE: SwissProt: O60260 # Defects in PARK2 are a cause of Parkinson disease (PD) [MIM:168600]. PD is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early- onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology of PD involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. & Defects in PARK2 are the cause of autosomal recessive early onset Parkinson disease 2 (PARK2) [MIM:600116]; also known as early-onset parkinsonism with diurnal fluctuation (EPDF) or autosomal recessive juvenile Parkinson disease (PDJ). PARK2 is symptomatically different in several aspects from idiopathic Parkinson disease, although classic symptoms such as bradykinesia, rigidity and tremor are present. Additional clinical features include early DOPA-induced dyskinesia, diurnal fluctuation of the symptoms, sleep benefit, dystonia and hyper-reflexia. PARK2 is usually characterized by onset before 40, with a mean age at onset of 23.2 years. Pathologically, PARK2 patients show loss of dopaminergic neurons in the substantia nigra, similar to that seen in Parkinson disease; however, Lewy bodies (intraneuronal accumulations of aggregated proteins) are absent. & Defects in PARK2 may be involved in the development and/or progression of ovarian cancer.
      SIMILARITY: Contains 2 IBR-type zinc fingers. & Contains 2 RING-type zinc fingers. & Contains 1 ubiquitin-like domain.
      MISCELLANEOUS: The parkin locus (PRKN), adjacent to the 6q telomere is hyper-recombinable and lies within FRA6E, the third most common fragile site in tumor tissue.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain at -20°C in undiluted aliquots for up to 12 months after date of receipt. Avoid repeated freeze/thaw cycles.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information


      Anti-Parkin Antibody, clone PRK8 SDS


      Safety Data Sheet (SDS) 

      Anti-Parkin Antibody, clone PRK8 Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-PARKIN - 2510330 2510330
      MOUSE ANTI-PARKIN - 3172124 3172124
      MOUSE ANTI-PARKIN - 3884777 3884777


      Reference overviewPub Med ID
      Increasing the Coding Potential of Genomes Through Alternative Splicing: The Case of PARK2 Gene.
      La Cognata, V; Iemmolo, R; D'Agata, V; Scuderi, S; Drago, F; Zappia, M; Cavallaro, S
      Current genomics  15  203-16  2014

      Show Abstract
      24955028 24955028
      Parkin differently regulates presenilin-1 and presenilin-2 functions by direct control of their promoter transcription.
      Duplan, E; Sevalle, J; Viotti, J; Goiran, T; Bauer, C; Renbaum, P; Levy-Lahad, E; Gautier, CA; Corti, O; Leroudier, N; Checler, F; da Costa, CA
      Journal of molecular cell biology  5  132-42  2013

      Show Abstract
      23359614 23359614
      S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson's disease
      Carmen R Sunico 1 , Tomohiro Nakamura, Edward Rockenstein, Michael Mante, Anthony Adame, Shing Fai Chan, Traci Fang Newmeyer, Eliezer Masliah, Nobuki Nakanishi, Stuart A Lipton
      Mol Neurodegener  8  29  2013

      Show Abstract
      23985028 23985028
      Co-regulation of intragenic microRNA miR-153 and its host gene Ia-2 β: identification of miR-153 target genes with functions related to IA-2β in pancreas and brain.
      Mandemakers, W; Abuhatzira, L; Xu, H; Caromile, LA; Hébert, SS; Snellinx, A; Morais, VA; Matta, S; Cai, T; Notkins, AL; De Strooper, B
      Diabetologia  56  1547-56  2013

      Show Abstract
      23595248 23595248
      Characterization of the Brain 26S Proteasome and its Interacting Proteins.
      Tai, HC; Besche, H; Goldberg, AL; Schuman, EM
      Frontiers in molecular neuroscience  3  2010

      Show Abstract Full Text Article
      20717473 20717473
      Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy.
      Fournier, M; Vitte, J; Garrigue, J; Langui, D; Dullin, JP; Saurini, F; Hanoun, N; Perez-Diaz, F; Cornilleau, F; Joubert, C; Ardila-Osorio, H; Traver, S; Duchateau, R; Goujet-Zalc, C; Paleologou, K; Lashuel, HA; Haass, C; Duyckaerts, C; Cohen-Salmon, C; Kahle, PJ; Hamon, M; Brice, A; Corti, O
      PloS one  4  e6629  2009

      Show Abstract
      19680561 19680561
      Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease.
      da Costa, CA; Sunyach, C; Giaime, E; West, A; Corti, O; Brice, A; Safe, S; Abou-Sleiman, PM; Wood, NW; Takahashi, H; Goldberg, MS; Shen, J; Checler, F
      Nature cell biology  11  1370-5  2009

      Show Abstract
      19801972 19801972
      Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death.
      Huynh, DP; Nguyen, DT; Pulst-Korenberg, JB; Brice, A; Pulst, SM
      Experimental neurology  203  531-41  2007

      Show Abstract
      17097639 17097639

      Data Sheet


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      Life Science Research > Antibodies and Assays > Primary Antibodies