Anti-Phospho-Parkin (Ser378) PARK2 Antibody

Parkin is an E3 ligase in the ubiquitin-proteasome system. Hereditary Parkinson’s disease is most commonly caused by mutations in the parkin gene and is characterized by the progressive loss of dopaminergic neurons and the presence of Lewy bodies in the substantia nigra (Jenner et al.,1992) . Recent evidence suggests that phosphorylation of parkin at Ser-378 may have an important regulatory role on its E3 ubiquitin ligase activity (Yamamoto et al., 2005) .

AR JP antibody, E3 ubiquitin ligase antibody, E3 ubiquitin protein ligase parkin antibody, E3 ubiquitin-protein ligase parkin antibody, FRA6E antibody, LPRS 2 antibody, LPRS2 antibody, PARK 2 antibody, Park2 antibody, Parkin 2 antibody, Parkinson disease (autosomal recessive juvenile) 2 antibody, Parkinson disease (autosomal recessive juvenile) 2 parkin antibody, Parkinson disease protein 2 antibody, Parkinson juvenile disease protein 2 antibody, Parkinson protein 2 E3 ubiquitin protein ligase antibody, Parkinson protein 2 E3 ubiquitin protein ligase (parkin) antibody, PDJ antibody, PRKN 2 antibody, PRKN antibody, PRKN2 antibody, PRKN2_HUMAN antibody, Ubiquitin E3 ligase PRKN antibody

Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser378 of human Parkin, conjugated to keyhole limpet hemocyanin (KLH) . Immunogen species is Human.

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 (at protein level) .

Cell Biology, Metabolism, Mitochondrial Metabolism, Neurodegenerative Disease, Neurology Process, Neuroscience, Pathways and Processes, Proteasome / Ubiquitin, Proteolysis/Ubiquitin, Ring Finger E3 Ligase, Ubiquitin E3 Enzymes

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 (PubMed:10973942, PubMed:10888878, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:16135753, PubMed:21376232, PubMed:23754282, PubMed:23620051, PubMed:24660806, PubMed:24751536) . Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25621951) . 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 (PubMed:17846173, PubMed:19229105) . Mediates 'Lys-63'- linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11590439, PubMed:11431533, PubMed:19229105, PubMed:11590439, PubMed:15728840) . Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974) . Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:23620051, PubMed:24896179, PubMed:25527291) . Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy (PubMed:25621951) . 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 (PubMed:21376232) . 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 (PubMed:22082830) . Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972) . May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185) . May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. After date of receipt, stable for at least 1 year at -20°C.

Cytoplasm, cytosol. Nucleus. Endoplasmic reticulum. Mitochondrion. Mainly localizes in the cytosol. Co-localizes with SYT11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. Mitochondrial localization gradually increases with cellular growth. Also relocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1- dependent.