Recombinant Human Serine/threonine-protein kinase PINK1, mitochondrial(PINK1),partial

Code CSB-YP863144HU
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Source Yeast
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Code CSB-EP863144HU
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Source E.coli
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Code CSB-EP863144HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP863144HU
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Source Baculovirus
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Code CSB-MP863144HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names PINK1
Uniprot No. Q9BXM7
Alternative Names
BRPK; FLJ27236; mitochondrial; PARK 6; PARK6; Phosphatase and Tensin Homolog; PINK 1; PINK1; PINK1_HUMAN; Protein kinase BRPK; PTEN induced putative kinase 1; PTEN induced putative kinase protein 1; PTEN-induced putative kinase protein 1; Serine/threonine kinase PINK1 mitochondrial; Serine/threonine protein kinase PINK1 mitochondrial; Serine/threonine-protein kinase PINK1
Species Homo sapiens (Human)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Serine/threonine-protein kinase which protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as PRKN and DNM1L, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components. 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. Mediates the translocation and activation of PRKN at the outer membrane (OMM) of dysfunctional/depolarized mitochondria. At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains at 'Ser-65', the PINK1-phosphorylated polyubiquitin then recruits PRKN from the cytosol to the OMM where PRKN is fully activated by phosphorylation at 'Ser-65' by PINK1. In damaged mitochondria, mediates the decision between mitophagy or preventing apoptosis by promoting PRKN-dependent poly- or monoubiquitination of VDAC1; polyubiquitination of VDAC1 by PRKN promotes mitophagy, while monoubiquitination of VDAC1 by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. When cellular stress results in irreversible mitochondrial damage, functions with PRKN to promote clearance of damaged mitochondria via selective autophagy (mitophagy). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by phosphorylating and thus promoting the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2. This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes. Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L. 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. Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10.
Gene References into Functions
  1. These results identify a novel role of PINK1 modulating the levels of LRRK2 in Parkinson's disease fibroblasts and neurons. PMID: 27975167
  2. Knockdown of PINK1 suppressed the proliferation, migration, invasion, and induced apoptosis and mitochondrial dysfunction of lung cancer cells. PMID: 29966978
  3. these findings suggest that CHIP plays a role in negative regulation of PINK1 stability and may suppress PINK1's cytoprotective effect during staurosporine-induced mammalian cell death. PMID: 29242192
  4. Results describe a novel pathogenic mechanism in recessive Parkinson's disease, where PINK1 deficiency may increase neuron death via exacerbation of inflammatory stimuli-induced nitric oxide production and abnormal innate immune responses in glia cells. PMID: 29321620
  5. The results demonstrate that Nix can serve as an alternative mediator of mitophagy to maintain mitochondrial turnover, identifying Nix as a promising target for neuroprotective treatment in PINK1/Parkin-related Parkinson's disease. PMID: 28281653
  6. Studies indicate a functional PTEN-induced putative kinase 1)(PINK1)/E3 ubiquitin protein ligase (parkin) mitophagy pathway in neurons [Review]. PMID: 29085955
  7. PINK1 detection could help stratify patients who may have poor response to chemotherapy and guide the individual treatment. PMID: 29937472
  8. A mitochondrial protein PINK1 acts as a mitochondrial gatekeeper able to sense the presence of healthy or damaged mitochondria. (Review) PMID: 28647367
  9. mitochondrial dysfunction activates the PINK1/Parkin signaling and mitophagy in renal tubular epithelial cells under albumin overload condition. PMID: 29494565
  10. High Pink1 Expression is Associated with Cancer Progression and Chemo-Resistance in Esophageal Squamous Cell Carcinoma. PMID: 29022200
  11. Hsp70participated in PINK1-mediated mitophagy by stabilizing PINK1. PMID: 29107085
  12. This study showed that the heterozygous Pink1 mutation carriers show subtle motor abnormalities when a detailed, specialized motor examination is applied and compared to mutation-negative matched control subjects. PMID: 28716427
  13. These findings provide evidence for a novel mechanism underlying the protective effects of PINK1 against alpha-syn-induced neurodegeneration and highlight a novel therapeutic target for Parkinson's disease treatment. PMID: 28933786
  14. Study confirmed that common variants in PARL and PINK1 were associated with leprosy. Furthermore, PARL and PINK1 could physically interact with each other and were involved in the highly connected network formed by reported leprosy susceptibility genes PMID: 27876828
  15. melatonin stimulates PINK1 expression via an MT2 /Akt/NF-kappaB pathway, and such stimulation is important for the prevention of neuronal cell apoptosis under high glucose conditions. PMID: 28580603
  16. The importance of parkin activation by the PINK1 phosphorylation. PMID: 28007983
  17. Target of PINK1 polyubiquitination is the mature form and is mediated by ubiquitination of a conserved lysine at position 137. PMID: 28683321
  18. that mutant PINK1 p.I368N can not be stabilized on the outer mitochondrial membrane upon mitochondrial stress and due to conformational changes in the active site does not exert kinase activity towards ubiquitin PMID: 28438176
  19. PINK1 mediates the complex balance between polyphyllin I-induced mitophagy and mitochondrial fission-mediated apoptosis in breast cancer cells. PMID: 28060722
  20. Here we review the evidence supporting PINK1/Parkin mitophagy in vivo and its causative role in neurodegeneration, and outline outstanding questions for future investigations. PMID: 28213158
  21. PINK1 utilises a lowly populated yet more suitable C-terminally retracted (Ub-CR) conformation of Ub for efficient phosphorylation. PMID: 29133469
  22. PINK1 was downregulated in the brains of patients with Alzheimer's disease. PMID: 29077793
  23. PINK1 mutation is associated with Alzheimer disease. PMID: 29091718
  24. PINK1 silencing impaired BECN1 enrichment at mitochondria-associated membranes independently of PARK2, suggesting a novel role for PINK1 in regulating mitophagy. PMID: 28368777
  25. an impaired PINK1-PARK2-mediated neuroimmunology pathway contributes to septic death. PMID: 27754761
  26. We demonstrated that miR-27a and miR-27b regulate PINK1 expression and autophagic clearance of damaged mitochondria PMID: 27456084
  27. The effects of variants in the Parkin, PINK1, and DJ-1 genes along with evidence for their pathogenicity have been summarized. (Review) PMID: 26965687
  28. data suggest that ROS may act as a trigger for the induction of Parkin/PINK1-dependent mitophagy. PMID: 28848050
  29. PKA-mediated phosphorylation of MIC60 negatively regulates mitochondrial clearance that is initiated by PINK1 and Parkin. PMID: 27153535
  30. We report that loss of PINK1 contributes to the Warburg effect through ROS-dependent stabilization of hypoxia-inducible factor-1A and reduced pyruvate kinase muscle isozyme 2 activity which highlight the importance of PINK1 and reactive oxygen species balance in normal and tumor cells. PMID: 27325644
  31. PINK1 disease mutants failed to recruit synphilin-1 and did not activate mitophagy, indicating that PINK1-synphilin-1-SIAH-1 represents a new parkin-independent mitophagy pathway. Drugs that activate this pathway will provide a novel strategy to promote the clearance of damaged mitochondria in Parkinson's disease. PMID: 27334109
  32. PINK1 p.G411S is a rare genetic risk factor with a relatively large effect size conferred by a partial dominant-negative function phenotype. PMID: 27807026
  33. In summary, our results demonstrate that PINK1 promoted hepatic IR via JNK and ERK pathway in PA treated HepG2 cells, implying a novel molecular target for the therapy of diabetes. PMID: 27423393
  34. the results suggest that BNIP3 plays a vital role in regulating PINK1 mitochondrial outer membrane localization, the proteolytic process of PINK1 and PINK1/parkin-mediated mitophagy under physiological conditions. PMID: 27528605
  35. PINK1 interferes with selective mitochondrial fission and mitophagy. PMID: 27091447
  36. findings suggest that PINK1 and PARKIN play critical roles in selective cell death in which damaged mitochondria are retained, independent of mitochondrial autophagy. PMID: 27302064
  37. findings underscore the importance of a mitophagy regulatory network of ATM and PINK1/Parkin and elucidate a novel mechanism by which ATM influences spermidine-induced mitophagy PMID: 27089984
  38. our findings indicate that PINK1 plays a significant role in NSCLC progression and chemoresistance, and highlights its potential role as a target in future anticancer therapies. PMID: 28259921
  39. Association of early onset Parkinson' and severe clinical signs with multiple alterations in PINK1 in Turkish patients. PMID: 27455133
  40. Data suggest that PPARG (peroxisome proliferator-activated receptor gamma) protects against insecticide-induced cytotoxicity/apoptosis by regulating PINK1 (PTEN induced putative kinase 1) expression in neurons, including dopaminergic neurons; the insecticide used in these experiments was deltamethrin; the neuroprotective agent was the hypoglycemic agent, rosiglitazone. PMID: 27553674
  41. These findings pinpoint PINK1-short form as a sensor of proteasomal activities that transduces the proteasomal impairment signal to the aggresome formation machinery. PMID: 27050454
  42. Differential submitochondrial localization of PINK1 serves as a molecular switch for mediating two distinct mitochondrial signaling pathways in maintenance of mitochondrial homeostasis. PMID: 26436374
  43. Processing and shuttling of PINK1 through mitochondria is conformed to at least three possible functional microcompartments for PINK1 activity (I, cytosol; II, outer mitochondrial membrane; III, inside mitochondria). PMID: 26046594
  44. results indicate that PINK1 expression is positively regulated by NRF2 and that the NRF2-PINK1 signaling axis is deeply involved in cell survival. PMID: 26555609
  45. High expression of PARK6 might lead to the occurrence of non-small-cell lung cancer. PMID: 26245297
  46. These results suggest that pyruvate is required for CCCP-induced PINK1/PARK2-mediated mitophagy. PMID: 26071202
  47. PINK1-PARK2 pathway-mediated mitophagy plays a key regulatory role in CSE-induced mitochondrial ROS production and cellular senescence in human bronchial epithelial cells PMID: 25714760
  48. mutant G309D PINK1 significantly reduced phosphorylation of GSK3beta at serine 9, suggesting that alterations in GSK3beta activity play an essential role in mutant G309D PINK1-induced tau phosphorylation at the PHF-1 site PMID: 25899925
  49. TGF-beta1 induces lung epithelial cell mitochondrial ROS and depolarization and stabilizes the key mitophagy initiating protein, PINK1 PMID: 25785991
  50. The results of the combined in silico simulations-based and experimental assay-based study indicates that PINK1-dependent Ser65 phosphorylation of Parkin is required for its activation and triggering of 'opening' conformations. PMID: 25849928

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Involvement in disease Parkinson disease 6 (PARK6)
Subcellular Location Mitochondrion outer membrane; Single-pass membrane protein. Mitochondrion inner membrane; Single-pass membrane protein. Cytoplasm, cytosol.
Protein Families Protein kinase superfamily, Ser/Thr protein kinase family
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.
Database Links

HGNC: 14581

OMIM: 168600

KEGG: hsa:65018

STRING: 9606.ENSP00000364204

UniGene: Hs.389171

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