PINK1 Antibody (YA4465)(PBS only)
(Synonyms: BRPK; PARK6)PINK1 Antibody (YA4465) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to PINK1.
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Host:
Mouse
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Isotype:
IgG
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Application:
IHC-P, FC, ELISA
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Reactivity :
Human
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|
| Dilution Ratio | 1:200-1:1000 | 1:200-1:400 | 1:10000 |
Product Details
PINK1 Antibody (YA4465) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to PINK1.
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Host Mouse
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 63 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.
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Calculated Molecular Weight Predicted band size: 63 kDa
Purified recombinant fragment of human PINK1 (AA: 112-273) expressed in E. Coli.
affinity purified.
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
PINK1 (PTEN-induced kinase 1) is a mitochondrial serine/threonine kinase that functions as a sensor of mitochondrial damage and a central regulator of mitochondrial quality control mechanisms.[1] Upon mitochondrial depolarization, PINK1 accumulates on the outer mitochondrial membrane rather than undergoing constitutive turnover, thereby marking dysfunctional mitochondria for selective removal.[2][3] Mechanistically, stabilized PINK1 phosphorylates both ubiquitin and the E3 ubiquitin ligase Parkin, initiating a ubiquitin-dependent mitophagy pathway that promotes recruitment of autophagic machinery to damaged mitochondria.[3][4] Through this PINK1-Parkin signaling axis, cells maintain mitochondrial homeostasis, limit accumulation of dysfunctional organelles, and support neuronal survival under cellular stress conditions.[1][3][5] The PINK1-mediated mitophagy pathway is strongly linked to neurodegenerative disease biology, particularly Parkinson’s disease, where mutations in PINK1 represent an established cause of autosomal recessive early-onset Parkinsonism.[6][7] Experimental studies further demonstrate that impaired PINK1-Parkin signaling results in defective mitochondrial clearance and accumulation of damaged mitochondria, whereas restoration of pathway activity promotes mitophagy and protects neurons from apoptosis in disease models.[5][8] Compared with related mitochondrial quality-control regulators, PINK1 is distinguished by its kinase-dependent damage-sensing function and its highly specific phosphorylation of ubiquitin, a critical upstream event required for efficient Parkin activation.[4] For experimental applications, genetic modulation of PINK1 expression and pharmacological enhancement of PINK1-Parkin-mediated mitophagy are widely used to investigate mitochondrial dysfunction, neurodegeneration, and mitochondrial quality-control mechanisms.[5][9]
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Subcellular Localization
Mitochondrion outer membrane; Single-pass membrane protein; Mitochondrion inner membrane; Single-pass membrane protein; Cytoplasm, cytosol
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Expression
Tissue_specificity:Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development -
Isoforms & Post-Translational Modification
Q9BXM7 has 2 isomers: Q9BXM7-1: 62769 Da (predicted); Q9BXM7-2: 30104 Da (predicted).
Proteolytically cleaved (PubMed:19229105, PubMed:22354088, PubMed:30733118). In healthy cells, the precursor is continuously imported into the inner mitochondrial membrane (IMM), where it is proteolytically cleaved by mitochondrial-processing peptidase (MPP) and then undergoes further proteolytic cleavage by PARL or AFG3L2 to give rise to the 52 kDa short form (PubMed:19229105, PubMed:22354088). The 52 kDa short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (PubMed:20404107). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) (PubMed:20404107, PubMed:30733118). If accumulation at the OMM fails and it is imported into the depolarized mitochondria, it undergoes cleavage by the IMM protease OMA1, promoting its subsequent degradation by the proteasome (PubMed:30733118);Autophosphorylated (PubMed:18957282, PubMed:20404107, PubMed:22910362). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation (PubMed:18957282, PubMed:20404107, PubMed:22910362). Autophosphorylation at Ser-228 and Ser-402 is sufficient and essential for selective recruitment of PRKN to depolarized mitochondria, via PINK1-dependent phosphorylation of ubiquitin and maybe PRKN (PubMed:18957282, PubMed:22910362) -
Subunit
Upon mitochondrial depolarization, it forms a supercomplex with TOM and TIM23 complexes (PubMed:38416681). PINK1-TOM-TIM23 supercomplex formation requires PINK1 interaction with TOMM20 and TOMM70 and is critical for PINK1 stabilization at the outer mitochondrial membrane, kinase activation and downstream mitophagy (PubMed:35391620, PubMed:38416681, PubMed:38848361). Upon mitochondrial depolarization, interacts with TIMM23; the interaction is required for PINK1 accumulation at the outer mitochondrial membrane, kinase activation by autophosphorylation and PRKN recruitement to mitochondria (PubMed:35391620, PubMed:37160114, PubMed:38416681, PubMed:38848361). Interacts with PRKN (PubMed:19966284, PubMed:20798600). Interacts with FBXO7 (PubMed:23933751). Forms a complex with PRKN and PARK7 (PubMed:19229105). Interacts with NENF (PubMed:31536960)
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SwissProt ID
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Synonyms
BRPK; PARK6
Documentation
References
[1]. Uniprotkb.
[2]. Jones N. PINK1 targets dysfunctional mitochondria for autophagy in Parkinson disease. Nat Rev Neurol. 2010 Apr;6(4):181. doi: 10.1038/nrneurol.2010.19. PMID: 20383881. et al. PINK1 targets dysfunctional mitochondria for autophagy in Parkinson disease. Nat Rev Neurol. 2010 Apr;6(4):181. [Content Brief]
[3]. Pickrell AM, et al. The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron. 2015 Jan 21;85(2):257-73. [Content Brief]
[4]. Sauvé V, et al. Phosphorylated ubiquitin: a new shade of PINK1 in Parkin activation. Cell Res. 2014 Sep;24(9):1025-6. [Content Brief]
[5]. Li J, et al. PINK1-parkin-mediated neuronal mitophagy deficiency in prion disease. Cell Death Dis. 2022 Feb 18;13(2):162. [Content Brief]
[6]. Wang S, et al. The mitophagy pathway and its implications in human diseases. Signal Transduct Target Ther. 2023 Aug 16;8(1):304. [Content Brief]
[7]. Masaldan S, et al. Therapeutic targeting of mitophagy in Parkinson's disease. Biochem Soc Trans. 2022 Apr 29;50(2):783-797. [Content Brief]
[8]. Deas E, et al. Mitophagy and Parkinson's disease: the PINK1-parkin link. Biochim Biophys Acta. 2011 Apr;1813(4):623-33. [Content Brief]
[9]. O'Callaghan B, et al. PINK1: From Parkinson's disease to mitophagy and back again. PLoS Biol. 2023 Jun 29;21(6):e3002196. [Content Brief]
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