Rabbit Parkin Polyclonal Antibody | anti-PRKN antibody

Parkin Antibody

Cat. Num. AAA9613522

• Gene Names: PARK2; PDJ; PRKN; AR-JP; LPRS2
• Reactivity: Human, Mouse, Rat
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin
• Synonyms: Parkin; Polyclonal Antibody; Parkin Antibody; AR JP; E3 ubiquitin ligase; E3 ubiquitin protein ligase parkin; E3 ubiquitin-protein ligase parkin; FRA6E; LPRS 2; LPRS2; PARK 2; Park2; Parkin 2; Parkinson disease (autosomal recessive juvenile) 2; Parkinson disease (autosomal recessive; juvenile) 2; parkin; Parkinson disease protein 2; Parkinson juvenile disease protein 2; Parkinson protein 2 E3 ubiquitin protein ligase; Parkinson protein 2; E3 ubiquitin protein ligase (parkin); PDJ; PRKN 2; PRKN; PRKN2; PRKN2_HUMAN; Ubiquitin E3 ligase PRKN; anti-PRKN antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Parkin Antibody detects endogenous levels of total Parkin.; 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. Found in serum (at protein level).
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-PRKN antibody: Peptide ELISA (EIA)
• Application Notes: Peptide ELISA: 1:20,000-1:40,000
• Immunogen: A synthesized peptide derived from human Parkin.
• Conjugation: Unconjugated
• Fragment: Fab fragment
• Post Translational Modifications: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. Also polyubiquitinated by RNF41 for proteasomal degradation. S-nitrosylated. The inhibition of PRKN ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in PD by impairing the ubiquitination of PRKN substrates.Phosphorylation at Ser-65 by PINK1 contributes to activate PRKN activity. It is however not sufficient and requires binding to phosphorylated ubiquitin as well.
• Subunit Structure: 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 PRKN, CUL1 and FBXW7. Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11. Interacts and regulates the turnover of SEPTIN5. 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 PRKN and GPR37, thus facilitating PRKN-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PRKN, whereas, STUB1 enhances the E3 activity of PRKN through promotion of dissociation of HSP70 from PRKN-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. Interacts with CHPF, the interaction with isoform 2 may facilitate PRKN transport into the mitochondria. Interacts with MFN2 (phosphorylated), promotes PRKN localization in dysfunctional depolarized mitochondria. Interacts with FBXO7; this promotes translocation to dysfunctional depolarized mitochondria. Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria. Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria. Forms a complex with PINK1 and PARK7.
• Similarity: The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes.The RING-type 1 zinc finger domain is required to repress p53/TP53 transcription.Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain (PubMed:21532592).Belongs to the RBR family. Parkin subfamily.
• Subcellular Location: Cytoplasm>Cytosol. Nucleus. Endoplasmic reticulum. Mitochondrion.; Note: 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.
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Related Product Information for anti-PRKN antibody

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, SEPTIN5, 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 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 a 22kDa 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 assembles '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.

NCBI and Uniprot Product Information

• NCBI GI #: 169790969
• NCBI GeneID: 5071
• NCBI Accession #: NP_004553.2
• NCBI GenBank Nucleotide #: NM_004562.2
• UniProt Accession #: O60260; Q5TFV8; Q6Q2I6; Q8NI41; Q8NI43; Q8NI44; Q8WW07; A3FG77; A8K975
• Molecular Weight: 51,641 Da
• NCBI Official Full Name: E3 ubiquitin-protein ligase parkin isoform 1
• NCBI Official Synonym Full Names: parkinson protein 2, E3 ubiquitin protein ligase (parkin)
• NCBI Official Symbol: PARK2
• NCBI Official Synonym Symbols: PDJ; PRKN; AR-JP; LPRS2
• NCBI Protein Information: E3 ubiquitin-protein ligase parkin; parkinson juvenile disease protein 2; Parkinson disease (autosomal recessive, juvenile) 2, parkin
• UniProt Protein Name: E3 ubiquitin-protein ligase parkin
• Protein Family: Parkin coregulated gene protein
• UniProt Gene Name: PARK2
• UniProt Synonym Gene Names: PRKN; Parkinson disease protein 2
• UniProt Entry Name: PRKN2_HUMAN

NCBI Description

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]

Uniprot Description

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 6.3.2.19; Ubiquitin conjugating system; Ubiquitin ligase; EC 6.3.2.-; Ligase

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

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

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

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

Disease: Parkinson Disease 2, Autosomal Recessive Juvenile; Leprosy, Susceptibility To, 2; Lung Cancer; Ovarian Cancer