Parkin Antibody (YA5898)

Cat. No.: HY-P86206: Data Sheet COA
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Parkin Antibody (YA5898) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Parkin.

For research use only. We do not sell to patients.

Size	Stock	Quantity
10 μL	In-stock	Estimated Time of Arrival: December 31
50 μL	In-stock	Estimated Time of Arrival: December 31
100 μL	In-stock	Estimated Time of Arrival: December 31
250 μL	Get quote

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Documentation

Description

Parkin Antibody (YA5898) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Parkin.

Host

Rabbit

Clonality

Monoclonal

Molecular Weight

Predicted band size: 52 kDa;

Observed band size: 52 kDa

Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.

Species Reactivity

Human, Mouse, Rat

SwissProt ID

O60260

Gene ID

5071 [NCBI]

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:2000-1:10000
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:200-1:1000
ELISA ELISA: Enzyme Linked Immunosorbent Assay	1:5000-1:20000

Purity	Protein A	Conjugation	Non-conjugated
Modification	Unmodified	Isotype	IgG,IgG/Kappa

Appearance

Liquid

Formulation

Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05% BSA

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Background

Function：Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, 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:25474007, PubMed:25621951, PubMed:32047033). 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:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). 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 (PubMed:12719539)

Subcellular Localization：Cytoplasm, cytosol; Nucleus; Endoplasmic reticulum; Mitochondrion; Mitochondrion outer membrane; Cell projection, neuron projection; Postsynaptic density; Presynapse

Expression：
Tissue_specificity:Highly expressed in the brain (including the substantia nigra) (PubMed:19501131, PubMed:9560156) . Also expressed in the heart, testes, and skeletal muscle (PubMed:9560156) . Downregulated or absent in tumor biopsy tissue, and not detected in the PARK2 brain (PubMed:12719539, PubMed:14614460) . Overexpression protects dopaminergic neurons from fumarate-mediated apoptosis (PubMed:12628165) . Detectable in serum (protein level) (PubMed:19501131) .

Isoforms & Post-Translational Modification：O60260 has 8 isomers: O60260-1: 51641 Da (predicted); O60260-2: 48713 Da (predicted); O60260-3: 23639 Da (predicted); O60260-4: 30616 Da (predicted); O60260-5: 42407 Da (predicted); O60260-6: 35631 Da (predicted); O60260-7: 43485 Da (predicted); O60260-8: 46413 Da (predicted).
ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates its E3 ligase activity;Auto-ubiquitinates in an E2-dependent manner leading to its own degradation (PubMed:19229105, PubMed:23770917, PubMed:25474007). Also polyubiquitinated by RNF41 for proteasomal degradation (PubMed:19229105);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;Phosphorylated (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Activation requires phosphorylation at Ser-65 by PINK1 and binding to PINK1 phosphorylated ubiquitin (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Phosphorylation at Thr-175 by PINK1 and at Thr-217 is important for mitochondrial localization (PubMed:18957282)

Subunit：Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6 (PubMed:11078524, PubMed:21532592). Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1. Part of a SCF-like complex, consisting of PRKN, CUL1 and FBXW7 (PubMed:12628165). Interacts with SNCAIP (PubMed:11590439, PubMed:15728840). Binds to the C2A and C2B domains of SYT11 (PubMed:12925569). Interacts and regulates the turnover of SEPTIN5 (PubMed:11078524). Part of a complex, including STUB1, HSP70 and GPR37 (PubMed:12150907). The amount of STUB1 in the complex increases during ER stress (PubMed:12150907). STUB1 promotes the dissociation of HSP70 from PRKN and GPR37, thus facilitating PRKN-mediated GPR37 ubiquitination (PubMed:12150907). 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 (PubMed:12150907). Interacts with PSMD4 and PACRG (PubMed:12634850, PubMed:14532270). Interacts with LRRK2 (PubMed:16352719). Interacts with RANBP2 (PubMed:16332688). Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination (PubMed:16955485). Interacts (via first RING-type domain) with AIMP2 (via N-terminus) (PubMed:16135753). Interacts with PSMA7 and RNF41 (PubMed:15987638, PubMed:18541373). Interacts with PINK1 (PubMed:19966284, PubMed:20798600). Forms a complex with PINK1 and PARK7 (PubMed:19229105). Interacts with CHPF, the interaction with isoform 2 may facilitate PRKN transport into the mitochondria (PubMed:22082830). Interacts with MFN2 (phosphorylated), promotes PRKN localization in dysfunctional depolarized mitochondria (PubMed:23620051). Interacts with FBXO7; this promotes translocation to dysfunctional depolarized mitochondria (PubMed:23933751). Interacts with ZNF746 (PubMed:21376232). Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria (PubMed:24270810). Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria (PubMed:24270810). Forms a complex with PRKN and PARK7 (PubMed:19229105). Interacts with AMBRA1 (By similarity)

Synonyms

PARK2; PRKN; E3 ubiquitin-protein ligase parkin; Parkinson juvenile disease protein 2; Parkinson disease protein 2

Documentation

Select Batch:

Data Sheet (235 KB) SDS (251 KB)

COA (205 KB)

User Guide for Antibodies (1077 KB)