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

Code CSB-YP863144HU
Size Pls inquire other sizes
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP863144HU
Size Pls inquire other sizes
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP863144HU-B
Size Pls inquire other sizes
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP863144HU
Size Pls inquire other sizes
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP863144HU
Size Pls inquire other sizes
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

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 full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
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.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°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.

Target Data

Function Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN
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
  51. Unravelling the regulatory mechanisms of PINK1 is essential for a full comprehension of its kinase function in health and disease. PMID: 25849930
  52. In this review, we summarize the biochemical mechanisms that underlie the association of PINK1 with mitochondria under normal and pathological conditions PMID: 25849931
  53. In the present review, we emphasize the functional overlap between the PINK1-Parkin pathway and the endoplasmic reticulum (ER)-mitochondria interface, a subcellular compartment critically involved in neurodegeneration. PMID: 25849933
  54. PINK1 variants are prevalent for causing Parkinson's disease in India PMID: 26282903
  55. Recessively inherited Parkin and PTEN-induced putative kinase 1 (PINK1) mutations have been investigated in this context and the present review describes the first insights gained from studies in iPSC-derived dopaminergic neurons PMID: 25849934
  56. PINK1 utilizes a mitochondrial localization mechanism that is distinct from that of conventional MTS proteins and that presumably functions in conjunction with the Tom complex in OMM localization when the conventional N-terminal MTS is inhibited. PMID: 25609704
  57. PINK1 phosphorylates Ser65 in both the Parkin ubiquitin-like domain and ubiquitin itself. These phosphorylation events cooperate to relieve the Parkin autoinhibition. PMID: 25700839
  58. This paper reports the first quantitative data on limb hypokinesia during gait in heterozygous PINK1 mutation carriers PMID: 25545816
  59. These data suggest that PINK1 positively regulates TG2 activity, which may be closely associated with aggresome formation in neuronal cells. PMID: 25557247
  60. PINK1 regulates mitochondrial respiratory function, reactive oxygen species generation, and mitochondrial transport. Moreover, recent studies implicate processed PINK1 in cytosolic signaling cascades that promote cell survival and neuron differentiation.[Review] PMID: 25557302
  61. Generated a complete structural model of human Parkin and studied phosphorylation of Parkin by PINK1. PMID: 25375667
  62. Cytosolic PINK1 is stabilized by TRAF6/NF-kappaB activation via Lys-63-linked ubiquitination. PMID: 25987559
  63. relationship between cancer rates and PD might be related to the involvement of common pathways in both diseases. This paper provides a concise overview on the cellular functions of the PINK1 and Parkin PMID: 25553463
  64. two receptors previously linked to xenophagy, NDP52 and optineurin, are the primary receptors for PINK1- and parkin-mediated mitophagy PMID: 26266977
  65. our results uncovered a mechanism by which PINK1-HDAC3 network mediates p53 inhibitory loop in response to oxidative stress-induced damage. PMID: 25305081
  66. Suggest a protective role of PINK1/Parkin-mediated mitophagy against chlorpyrifos-induced neuroapoptosis. PMID: 26070385
  67. The PINK1 p.Q456X mutation leads to a decrease in mRNA and a loss of protein function PMID: 25226871
  68. PINK1 phosphorylates both Ser65 (S65) in the UB(ubiquitin)-like domain of PARKIN and the conserved Ser in UB itself. PMID: 25969509
  69. Parkin, PINK1, and alpha-Synuclein have roles in stress-induced mitochondrial morphological remodeling, which may have a role in Parkinson's disease PMID: 25861987
  70. These results provide new insights into potential cooperative roles of PINK1 and PGC-1alpha in mitochondrial fatty acid oxidation, suggesting possible regulatory roles for mitochondrial function in the pathogenesis of Alzheimer disease and diabetes. PMID: 25260493
  71. PINK1 has tumor-promoting properties and PINK1 functions as a regulator of the cell cycle. PMID: 24681957
  72. This reported the first follow-up evaluation of motor and nonmotor clinical features in PINK1 mutation carriers. PMID: 25164310
  73. Cells lacking Pink1 were more sensitive to cell death induced by C2-Ceramide. In the same cell lines, mitochondrial morphology was fragmented by forskolin. Pink1 may exert a neuroprotective role in part by limiting mitochondrial fission. PMID: 24792327
  74. The functional interaction of mortalin with Parkin and PINK1, was investigated. PMID: 24743735
  75. PINK1 mutations linked with neurogeneration on Guam. PMID: 25558820
  76. our data identify ATP as a key regulator for Parkin mitochondrial translocation and sustaining elevated PINK1 levels during mitophagy. PINK1 functions as an AND gate and a metabolic sensor coupling biogenetics of cells PMID: 25404737
  77. Cells exposed to severe and irreparable mitochondrial damage agents such as valinomycin can undergo PINK1-Parkin-dependent apoptosis. The proapoptotic response elicited by valinomycin is associated with the degradation of Mcl-1. PMID: 25088558
  78. Data clarify the regulation of PINK1 through multisite phosphorylation. PMID: 25527497
  79. PINK1 expression is tightly regulated at its transcription level and NFkappaB is a positive regulator for PINK1 expression. PMID: 25108683
  80. data indicate that PINK1 deficiency results in swollen, dysfunctional mitochondria and defective mitophagy, and promotes fibrosis in the aging lung. PMID: 25562319
  81. The discovery of mutations in genes encoding protein kinase PTEN-induced kinase 1 (PINK1) and E3 ubiquitin ligase Parkin in familial Parkinson's disease PMID: 25345844
  82. Augmenting mitophagy by activating the PINK1/Parkin pathway is an attractive target for therapeutic intervention for Parkinson disease and a variety of maternally inherited mitochondrial diseases. PMID: 25611507
  83. This study shows that PARK13 and PINK1 are subcellular-specific, but dynamic, proteins with a reciprocal molecular relationship. PMID: 24798695
  84. the phosphorylation activity seen in PINK1 and PARKIN can differentiate between age-matched controls and Parkinson's disease patients PMID: 24962176
  85. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades. PMID: 25217637
  86. PINK1G309D, the loss-of-function mutation associated with early-onset familial Parkinson's disease, promotes expression of VCAM-1 and exacerbates attachment of monocytes to brain endothelial cells. PMID: 24385196
  87. Results show that PINK1 dependent phosphorylation signaling may regulate nuclear activities. PMID: 24626860
  88. the PINK1-mediated reduction of autophagic key factors during stress resulted in increased cell death. PMID: 24751806
  89. high prevalence of heterozygous mutations in PARK2 and the novel heterozygous and homozygous point mutations in PINK1 observed in familial and sporadic cases from various states of Mexico PMID: 24677602
  90. Our findings highlight a potential novel function of extramitochondrial PINK1 in dopaminergic neurons PMID: 24374372
  91. BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradation. PMID: 24475098
  92. These results indicate that association of PINK1 with SARM1 and TRAF6 is an important step for mitophagy. PMID: 23885119
  93. PINK1 expression is significantly increased upon CCCP-induced mitophagy in a calcium-dependent manner. PINK1 may play a role in mitophagy that is downstream of ubiquitination of mitochondrial substrates PMID: 24184327
  94. Two distinct cellular pools of PINK1 have different effects on Parkin translocation and mitophagy. PMID: 24357652
  95. results show that PINK1-dependent phosphorylation of both parkin and ubiquitin is sufficient for full activation of parkin E3 activity; findings demonstrate that phosphorylated ubiquitin is a parkin activator PMID: 24784582
  96. The expression of unfolded proteins in the matrix causes the accumulation of PINK1 on energetically healthy mitochondria, resulting in mitochondrial translocation of PARK2, mitophagy and subsequent reduction of unfolded protein load. PMID: 24149988
  97. PINK1 steady-state elimination by the N-end rule identifies a novel organelle to cytoplasm turnover pathway that yields a mechanism to flag damaged mitochondria for autophagic elimination. PMID: 24121706
  98. PINK1 controls parkin activity by phosphorylating parkin at serine-65. PMID: 24660806
  99. These results explain a feed-forward mechanism of PINK1-mediated initiation of Parkin E3 ligase activity. PMID: 24751536
  100. Our data support a novel role for PINK1 in regulating dendritic morphogenesis. PMID: 24151868

Show More

Hide All

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

Most popular with customers

Newsletters

Get all the latest information on Events, Sales and Offers. Sign up for newsletter today.

Copyright © 2007-2018 www.cusabio.com CUSABIO TECHNOLOGY LLC All Rights Reserved. 鄂ICP备15011166号-1