PINK1 Antibody (YA4465)

Cat. No.: HY-P84768: Data Sheet COA
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PINK1 Antibody (YA4465) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to PINK1.

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
References

Description

PINK1 Antibody (YA4465) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to PINK1.

Host

Mouse

Clonality

Monoclonal

Molecular Weight

Predicted band size: 63 kDa;

Observed 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.

Species Reactivity

Human

SwissProt ID

Q9BXM7

Gene ID

65018 [NCBI]

Immunogen

Purified recombinant fragment of human PINK1 (AA: 112-273) expressed in E. Coli.

Application &
Dilution Ratio

Application	Dilution Ratio
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:200-1:1000
FC FC: Flow Cytometry	1:200-1:400
ELISA ELISA: Enzyme Linked Immunosorbent Assay	1:10000

Purity	affinity purified.	Conjugation	Non-conjugated
Modification	Unmodified	Isotype	IgG1

Appearance

Liquid

Formulation

Supplied in PBS with 0.05% sodium azide

Storage & Stability

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

Shipping

Shipping with blue ice.

Background

Function：Serine/threonine-protein kinase which acts as a sensor of mitochondrial damage and protects against mitochondrial dysfunction during cellular stress. It phosphorylates mitochondrial proteins to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:14607334, PubMed:15087508, PubMed:18443288, PubMed:18957282, PubMed:19229105, PubMed:19966284, PubMed:20404107, PubMed:20547144, PubMed:20798600, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:24896179, PubMed:24898855, PubMed:25527291, PubMed:32484300). Depending on the severity of mitochondrial damage, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to eliminating severely damaged mitochondria via PINK1-PRKN-dependent mitophagy (PubMed:14607334, PubMed:15087508, PubMed:18443288, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24898855, PubMed:32047033, PubMed:32484300). When cellular stress results in irreversible mitochondrial damage, PINK1 accumulates at the outer mitochondrial membrane (OMM) where it phosphorylates pre-existing polyubiquitin chains at 'Ser-65', recruits PRKN from the cytosol to the OMM and activates PRKN by phosphorylation at 'Ser-65'; activated PRKN then ubiquinates VDAC1 and other OMM proteins to initiate mitophagy (PubMed:14607334, PubMed:15087508, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25474007, PubMed:25527291, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria through phosphorylation and PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:18443288, PubMed:23620051, PubMed:24898855). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:18443288, PubMed:23620051). Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L (PubMed:18443288, PubMed:32484300). Regulates motility of damaged mitochondria by promoting 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). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity). Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity (PubMed:29123128)

Subcellular Localization：Mitochondrion outer membrane; Single-pass membrane protein; Mitochondrion inner membrane; Single-pass membrane protein; Cytoplasm, cytosol

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)

RRID

AB_3718982

Synonyms

BRPK; PARK6

Documentation

Select Batch:

Data Sheet (234 KB) SDS (251 KB)

COA (205 KB)

User Guide for Antibodies (1077 KB)

References

[1]. /biology-dictionary/hcc827-cell.html [Content Brief]