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The precise function of PARK2 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. Additionally we are shipping PARK2 Antibodies (194) and PARK2 Kits (21) and many more products for this protein.
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Loss of parkin is associated with nuclear clustering and morphology defects in larval muscles and thus developing aortic aneurysms.
This study found learning and memory abnormalities in Parkin mutant genotypes in Drosophila.
parkin mutants have a longer lifespan when fed the 1:16 P:C compared to those fed the 1:2 P:C diet. Parkin mutants fed the 1:16 P:C diet have delayed climbing deficit, increased resistance to starvation. Mutant flies fed the 1:16 P:C diet also have improved mitochondrial functions as evidenced by increased respiratory control ratio
Drosophila CHIP protects against mitochondrial dysfunction by acting downstream of Pink1 (show PINK1 Proteins) in parallel with Parkin
Maintenance of tissue homeostasis upon reduction of Pink1 (show PINK1 Proteins) or Parkin appears to result from reduction of age- and stress-induced intestinal stem cell proliferation, in part, through induction of ISC senescence.
activation of endoplasmic reticulum stress by defective mitochondria is neurotoxic in pink1 (show PINK1 Proteins) and parkin flies and that the reduction of this signalling is neuroprotective, independently of defective mitochondria.
Pharmacological or genetic activation of heat shock protein 70 (Hsp70) protects against loss of parkin Function. Heat shock protein members may act as compensatory factors for parkin loss of function and that the exploitation of these factors may be of potential therapeutic value.
autophosphorylation of PINK1 (show PINK1 Proteins) is essential for the mitochondrial translocation of Parkin and for subsequent phosphorylation and activation of Parkin.
Our data indicate that PINK1 (show PINK1 Proteins) and Parkin play an important role in FUS (show FUS Proteins)-induced neurodegeneration. This study has uncovered a previously unknown link between FUS (show FUS Proteins) proteinopathy and PINK1 (show PINK1 Proteins)/Parkin genes, providing new insights into the pathogenesis of FUS (show FUS Proteins) proteinopathy.
Clu (show CLU Proteins) is upstream of and binds to VCP (show vcp Proteins) in vivo and promotes VCP (show vcp Proteins)-dependent Marf (show MFN2 Proteins) degradation in vitro Marf (show MFN2 Proteins) accumulates in whole muscle lysates of clu (show CLU Proteins)-deficient flies and is destabilized upon Clu (show CLU Proteins) overexpression. Thus, Clu (show CLU Proteins) is essential for mitochondrial homeostasis and functions in concert with Parkin and VCP (show vcp Proteins) for Marf (show MFN2 Proteins) degradation to promote damaged mitochondrial clearance.
mitochondrial dysfunction activates the PINK1 (show PINK1 Proteins)/Parkin signaling and mitophagy in renal tubular epithelial cells under albumin (show ALB Proteins) overload condition.
The authors demonstrate that RABGEF1 (show RABGEF1 Proteins), the upstream factor of the endosomal Rab GTPase (show RAB6A Proteins) cascade, is recruited to damaged mitochondria via ubiquitin binding downstream of Parkin. RABGEF1 (show RABGEF1 Proteins) directs the downstream Rab (show HRB Proteins) proteins, RAB5 (show RAB5A Proteins) and RAB7A (show RAB7A Proteins), to damaged mitochondria, whose associations are further regulated by mitochondrial Rab (show HRB Proteins)-GAPs.
DNAJ (show DNAJB6 Proteins) proteins keep Parkin C289G mutant protein in a soluble, degradation-competent form.
S-nitrosylated PINK1 (show PINK1 Proteins) decreases Parkin translocation to mitochondrial membranes
Parkinsonism associated with Parkin gene mutation is one of the most common familial forms of Parkinson Disease, which is characterized by early onset of symptoms, slow progression, elective dopaminergic neuronal loss and the absence of Lewy bodies.
A transcriptional repressor network including THAP domain containing 11 protein (THAP11) was identified and negatively regulates endogenous PARKIN abundance.
Study explored the role of parkin proteins in Parkinson's disease (PD) neurodegeneration by analyzing their expression profile in an in vitro model exposed to divers neurotoxins. Results showed that up- or down-regulation of specific splice isoforms may be a direct effect of toxin exposure. Moreover, the isoforms may exert different actions in neurodegeneration via modulation of different molecular pathways.
Mutations in the PARK2 gene were detected in four of the six tested families with a history of early-onset Parkinson disease.
This study showed that the heterozygous Parkin mutation carriers show subtle motor abnormalities when a detailed, specialized motor examination is applied and compared to mutation-negative matched control subjects.
The methylation of SNCA and PARK2 promoter regions were significantly lower in early-onset Parkinson's disease patients compared to control group. Methylation status of the SNCA might be associated with positive family history of Parkinson's disease.
Melatonin, added together with MPTP (show PTPN2 Proteins) or added once MPTP (show PTPN2 Proteins) was removed, prevented and recovered, respectively, the parkinsonian phenotype once it was established, restoring gene expression and normal function of the parkin/PINK1 (show PINK1 Proteins)/DJ-1 (show PARK7 Proteins)/MUL1 loop and also the normal motor activity of the embryos.
Single nucleotide polymorphism (SNP) analysis revealed seven SNPs in the porcine PARK2 gene, one missense and one silent mutation in exon 7 and five SNPs in intron 7
PINK1 (show PINK1 Proteins) and PARK2 suppress pancreatic tumorigenesis through control of mitochondrial iron-mediated immunometabolism
When fed with iron-supplemented diet, DMT1 (show SLC11A2 Proteins)-expressing mice exhibit rather selective accumulation of iron in the substantia nigra but otherwise seem normal. Parkin expression is also enhanced, likely as a neuroprotective response. When DMT1 (show SLC11A2 Proteins) is overexpressed against a Parkin null background, the double-mutant mice similarly resisted a disease phenotype when fed with iron or manganese, but greater susceptibility to 6-OHDA.
Bnip3l (show BNIP3L Proteins) knockout (bnip3l (show BNIP3L Proteins)(-/-)) impaired mitophagy and aggravated cerebral I-R (ischemia-reperfusion) injury in mice, which can be rescued by BNIP3L (show BNIP3L Proteins) overexpression. The rescuing effects of BNIP3L (show BNIP3L Proteins) overexpression can be observed in park2(-/-) mice, which showed mitophagy deficiency after I-R.
Parkin acts as a regulator of microtubule system during neuronal aging.
The expression of PINK1 (show PINK1 Proteins) and Parkin were elevated in white adipose tissue in obese mice.
crossed Parkin knockouts to the Twinkle-TG mouse in which mtDNA deletions are increased specifically in substantia nigra to determine the effect of increased deletion mutagenesis in the absence of mitochondrial quality control
These findings reveal parkin-mediated cytoprotective mechanisms against misfolded SOD1 (show SOD1 Proteins) toxicity.
Park2 deficiency exacerbates ethanol-induced dopaminergic neuron damage through p38 (show CRK Proteins) kinase dependent inhibition of autophagy and mitochondrial function.
PARK2-dependent acidic postconditioning -induced mitophagy renders the brain resistant to ischemic injury.
Our results indicate that strict maternal transmission of mitochondria relies on mitophagy and uncover a collaboration between MUL1 (show MUL1 Proteins) and PARKIN in this process.
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.
, E3 ubiquitin-protein ligase parkin
, Parkinson disease (autosomal recessive, juvenile) 2, parkin
, parkinson juvenile disease protein 2
, parkin variant SV5DEL
, parkin protein
, parkinson protein 2, E3 ubiquitin protein ligase (parkin)