AB5112 Anti-Parkin Antibody, a.a. 305-323

50 µL  
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      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, RELISA, WB, IHCRbSerumPolyclonal Antibody
      Catalogue NumberAB5112
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Parkin Antibody, a.a. 305-323
      Product Information
      PresentationRabbit serum. Lyophilized. Reconstitute with 50 μL of sterile distilled water. Centrifuge to remove insoluble material. Contains no preservative.
      Quality LevelMQ100
      ApplicationDetect Parkin using this Anti-Parkin Antibody, a.a. 305-323 validated for use in ELISA, WB, IH.
      Key Applications
      • ELISA
      • Western Blotting
      • Immunohistochemistry
      Application NotesImmunohistochemistry: 1:1000 - 1:2000

      One site ELISA

      Western blot: 1:1000 - 1:2000 (recognizes a doublet at 44-52 kDa on blots of human brain)

      The immunogen peptide is available (cat# AG237) for pre-absorbtion controls.

      Optimal working dilutions must be determined by the end user.
      Biological Information
      ImmunogenA 19 amino acid peptide (RILGEEQYNRYQQYGAEEC) corresponding to amino acids 305-323 of the human parkin molecule. An internal peptide sequence was chosen to avoid the possibility of cross reactivity with ubiquitin.
      Epitopea.a. 305-323
      SpecificityParkin. Parkinson's disease is a common neurodegenerative disease is caused by slow death of neurons in the substantial nigra, a brain region that utilizes the neurotransmitter dopamine. Parkin, a recently discovered gene encoding a large protein, may be involved in normal and abnormal protein degradation in cells. Recent evidence indicates that point mutations in the Parkin gene appear to be responsible for the pathogenesis of some forms of Parkinson's disease.
      Species Reactivity
      • Human
      • Rat
      Antibody TypePolyclonal 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 lyophilized material at at -20°C to -70°C for up to 12 months after date of receipt. After reconstitution maintain at -20°C to -70°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles. Glycerol (ACS grade or better) can be added (1:1) for greater stability.
      Packaging Information
      Material Size50 µL
      Transport Information
      Supplemental Information


      Anti-Parkin Antibody, a.a. 305-323 SDS


      Safety Data Sheet (SDS) 

      Anti-Parkin Antibody, a.a. 305-323 Certificates of Analysis

      TitleLot Number
      RABBIT ANTI-PARKIN - 24922082492208
      RABBIT ANTI-PARKIN - 34303033430303
      RABBIT ANTI-PARKIN -27818602781860
      RABBIT ANTI-PARKIN -28429192842919


      Reference overviewApplicationPub 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
      Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance.
      Lonskaya, I; Hebron, ML; Desforges, NM; Schachter, JB; Moussa, CE
      Journal of molecular medicine (Berlin, Germany)  92  373-86  2014

      Show Abstract
      24337465 24337465
      Decreased parkin solubility is associated with impairment of autophagy in the nigrostriatum of sporadic Parkinson's disease.
      Lonskaya, I; Hebron, ML; Algarzae, NK; Desforges, N; Moussa, CE
      Neuroscience  232  90-105  2013

      Show Abstract
      23262240 23262240
      Tyrosine kinase inhibition increases functional parkin-Beclin-1 interaction and enhances amyloid clearance and cognitive performance.
      Lonskaya, I; Hebron, ML; Desforges, NM; Franjie, A; Moussa, CE
      EMBO molecular medicine  5  1247-62  2013

      Show Abstract
      Immunohistochemistry23737459 23737459
      Parkin expression profile in dopamine d3 receptor knock-out mice brains.
      Velia D'Agata,Adriana Tiralongo,Alessandro Castorina,Gian Marco Leggio,Vincenzo Micale,Maria Luisa Carnazza,Filippo Drago
      Neurochemical research  34  2009

      Show Abstract
      18612813 18612813
      Parkin is expressed in vascular endothelial cells.
      Wakako Tamo, Tadaatsu Imaizumi, Kunikazu Tanji, Hidemi Yoshida, Shingo Takanashi, Koichi Wakabayashi, Ryosuke Takahashi, Nobutaka Hattori, Kei Satoh
      Neuroscience letters  419  199-201  2007

      Show Abstract
      17481813 17481813
      Parkinson's disease transgenic mitochondrial cybrids generate Lewy inclusion bodies.
      Trimmer, Patricia A, et al.
      J. Neurochem., 88: 800-12 (2004)  2004

      Show Abstract
      14756800 14756800
      Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age.
      Pawlyk, AC; Giasson, BI; Sampathu, DM; Perez, FA; Lim, KL; Dawson, VL; Dawson, TM; Palmiter, RD; Trojanowski, JQ; Lee, VM
      The Journal of biological chemistry  278  48120-8  2003

      Show Abstract
      12972409 12972409
      Alterations in the common fragile site gene Parkin in ovarian and other cancers.
      Denison, SR; Wang, F; Becker, NA; Schüle, B; Kock, N; Phillips, LA; Klein, C; Smith, DI
      Oncogene  22  8370-8  2003

      Show Abstract
      14614460 14614460
      Genomic organization and expression of parkin in Drosophila melanogaster.
      Bae, YJ; Park, KS; Kang, SJ
      Experimental & molecular medicine  35  393-402  2003

      Show Abstract
      14646593 14646593

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