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Recombinant Human PINK1 protein (denatured) is a Human Fragment protein, in the 156 to 507 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.

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Images

SDS-PAGE - Recombinant Human PINK1 protein (denatured) (AB116177), expandable thumbnail

Key facts

Purity
>90% SDS-PAGE
Expression system
Escherichia coli
Tags
Tag free
Applications
SDS-PAGE
Biologically active
No

Amino acid sequence

M Y L I G Q S I G K G C S A A V Y E A T M P T L P Q N L E V T K S T G L L P G R G P G T S A P G E G Q E R A P G A P A F P L A I K M M W N I S A G S S S E A I L N T M S Q E L V P A S R V A L A G E Y G A V T Y R K S K R G P K Q L A P H P N I I R V L R A F T S S V P L L P G A L V D Y P D V L P S R L H P E G L G H G R T L F L V M K N Y P C T L R Q Y L C V N T P S P R L A A M M L L Q L L E G V D H L V Q Q G I A H R D L K S D N I L V E L D P D G C P W L V I A D F G C C L A D E S I G L Q L P F S S W Y V D R G G N G C L M A P E V S T A R P G P R A V I D Y S K A D A W A V G A I A Y E I F G L V N P F Y G Q G K A H L E S R S Y Q E A Q L P A L P E S V P P D V R Q L V R A L L Q R E A S K R P S A R V A A N V L

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Target data

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).

Alternative names

Recommended products

Recombinant Human PINK1 protein (denatured) is a Human Fragment protein, in the 156 to 507 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.

Key facts

Purity
>90% SDS-PAGE
Expression system
Escherichia coli
Applications
SDS-PAGE
Accession
Q9BXM7-1
Animal free
No
Species
Human
Concentration
Loading...
Storage buffer

pH: 8
Constituents: 6.01% Urea, 5% Glycerol (glycerin, glycerine), 0.32% Tris HCl

Sequence info

Amino acid sequence

M Y L I G Q S I G K G C S A A V Y E A T M P T L P Q N L E V T K S T G L L P G R G P G T S A P G E G Q E R A P G A P A F P L A I K M M W N I S A G S S S E A I L N T M S Q E L V P A S R V A L A G E Y G A V T Y R K S K R G P K Q L A P H P N I I R V L R A F T S S V P L L P G A L V D Y P D V L P S R L H P E G L G H G R T L F L V M K N Y P C T L R Q Y L C V N T P S P R L A A M M L L Q L L E G V D H L V Q Q G I A H R D L K S D N I L V E L D P D G C P W L V I A D F G C C L A D E S I G L Q L P F S S W Y V D R G G N G C L M A P E V S T A R P G P R A V I D Y S K A D A W A V G A I A Y E I F G L V N P F Y G Q G K A H L E S R S Y Q E A Q L P A L P E S V P P D V R Q L V R A L L Q R E A S K R P S A R V A A N V L
Accession
Q9BXM7
Protein length
Fragment
Predicted molecular weight
37.9 kDa
Amino acids
156 to 507
Nature
Recombinant

Specifications

Form
Liquid
Additional notes

ab116177 was purified using conventional chromatography.

General info

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).

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Post-translational modifications

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).

Subcellular localisation
Mitochondrion outer membrane, Mitochondrion inner membrane

Storage

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

The PTEN-induced kinase 1 (PINK1) is a serine/threonine-protein kinase with a molecular weight of approximately 63 kDa. It plays a significant role in mitochondrial quality control through its kinase activity. PINK1 gets expressed in various tissues with a high presence in the brain. The protein localizes to the outer membrane of damaged mitochondria to initiate mitophagy an important cellular process for clearing dysfunctional mitochondria.

Biological function summary

The PINK1 protein detects mitochondrial damage and recruits Parkin an E3 ubiquitin ligase to the damaged mitochondria. This interaction leads to the ubiquitylation of mitochondrial substrates and triggers their degradation. PINK1 Parkin and other proteins form a complex that facilitates the removal of damaged mitochondria through autophagy. This mechanism ensures cellular health and energy balance by maintaining a pool of functional mitochondria.

Pathways

PINK1 integrates into the mitochondrial quality control and mitophagy pathways. It has a fundamental role in the PINK1-Parkin pathway which is critical for maintaining mitochondrial integrity. In this pathway PINK1 phosphorylates both ubiquitin and Parkin enhancing Parkin’s E3 ligase activity. Another pathway that PINK1 participates in is the PTEN-induced kinase pathway where it regulates mitochondrial dynamics and homeostasis via cross-talk with other mitochondrial proteins such as DJ-1 and LRRK2.

Associated diseases and disorders

PINK1 mutations are strongly associated with familial Parkinson’s disease attributing to its role in preserving neuronal function through mitochondrial regulation. Deficient PINK1 function leads to accumulation of damaged mitochondria contributing to neuronal cell death. Additionally PINK1 dysfunction is implicated in Alzheimer’s disease as impaired mitochondrial clearance is a contributing factor. Here the PINK1 interaction with other proteins like Parkin and DJ-1 highlights its importance in neurodegenerative disorders.

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1 product image

  • SDS-PAGE - Recombinant Human PINK1 protein (denatured) (ab116177), expandable thumbnail

    SDS-PAGE - Recombinant Human PINK1 protein (denatured) (ab116177)

    ab116177 on a 15% SDS-PAGE (3ug)

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