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PINK1 encodes a serine/threonine protein kinase that localizes to mitochondria. Additionally we are shipping PINK1 Proteins (13) and and many more products for this protein.
Showing 10 out of 238 products:
Human Polyclonal PINK1 Primary Antibody for ELISA, ICC - ABIN249446
Weihofen, Ostaszewski, Minami, Selkoe: Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. in Human molecular genetics 2008
Show all 85 Pubmed References
Human Polyclonal PINK1 Primary Antibody for WB - ABIN151937
Meijer, Karimi-Busheri, Huang, Weinfeld, Young: Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe. in The Journal of biological chemistry 2002
Show all 5 Pubmed References
Human Polyclonal PINK1 Primary Antibody for WB - ABIN1882117
Rogaeva, Johnson, Lang, Gulick, Gwinn-Hardy, Kawarai, Sato, Morgan, Werner, Nussbaum, Petit, Okun, McInerney, Mandel, Groen, Fernandez, Postuma, Foote: Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. in Archives of neurology 2004
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Human Polyclonal PINK1 Primary Antibody for SimWes, WB - ABIN152067
Xiong, Wang, Chen, Choo, Ma, Tang, Xia, Jiang, Ronai, Zhuang, Zhang: Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. in The Journal of clinical investigation 2009
Show all 3 Pubmed References
Human Monoclonal PINK1 Primary Antibody for IHC, WB - ABIN2115285
Zhou, Huang, Shao, May, Prou, Perier, Dauer, Schon, Przedborski: The kinase domain of mitochondrial PINK1 faces the cytoplasm. in Proceedings of the National Academy of Sciences of the United States of America 2008
Show all 2 Pubmed References
Human Polyclonal PINK1 Primary Antibody for ELISA, WB - ABIN566297
Liu, Ye, Miller, Yuan, Zhang, Tian, Nie, Imae, Arai, Li, Cheng, Shi: Ablation of ALCAT1 mitigates hypertrophic cardiomyopathy through effects on oxidative stress and mitophagy. in Molecular and cellular biology 2012
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Human Polyclonal PINK1 Primary Antibody for WB - ABIN652208
Berthier, Jiménez-Sáinz, Pulido: PINK1 regulates histone H3 trimethylation and gene expression by interaction with the polycomb protein EED/WAIT1. in Proceedings of the National Academy of Sciences of the United States of America 2013
Human Monoclonal PINK1 Primary Antibody for ICC, IF - ABIN4345677
Ko, Park, Park, Koh: PPAR-γ activation attenuates deltamethrin-induced apoptosis by regulating cytosolic PINK1 and inhibiting mitochondrial dysfunction. in Toxicology letters 2016
Maintenance of tissue homeostasis upon reduction of Pink1 or Parkin (show PARK2 Antibodies) appears to result from reduction of age- and stress-induced intestinal stem cell proliferation, in part, through induction of ISC senescence.
activation of endoplasmic reticulum stress by defective mitochondria is neurotoxic in pink1 and parkin (show PARK2 Antibodies) flies and that the reduction of this signalling is neuroprotective, independently of defective mitochondria.
autophosphorylation of PINK1 is essential for the mitochondrial translocation of Parkin (show PARK2 Antibodies) and for subsequent phosphorylation and activation of Parkin (show PARK2 Antibodies).
A pink1 genomic knock-in allele was generated to monitor the dynamic expression pattern of PINK1. The spatiotemporal expression pattern of PINK1 correlates with the cell-type specific mitochondrial clearance or persistence. PINK1 and PARKIN (show PARK2 Antibodies) function epistatically to mediate timely specific mitophagy during Drosophila midgut metamorphosis.
Our data indicate that PINK1 and Parkin (show PARK2 Antibodies) play an important role in FUS (show FUS Antibodies)-induced neurodegeneration. This study has uncovered a previously unknown link between FUS (show FUS Antibodies) proteinopathy and PINK1/Parkin (show PARK2 Antibodies) genes, providing new insights into the pathogenesis of FUS (show FUS Antibodies) proteinopathy.
we show that overexpression of Drosophila Clu (show CLU Antibodies) complements PINK1, but not parkin (show PARK2 Antibodies), mutant muscles. Thus, Clu (show CLU Antibodies) is essential for mitochondrial homeostasis and functions in concert with Parkin (show PARK2 Antibodies) and VCP (show vcp Antibodies) for Marf (show MFN2 Antibodies) degradation to promote damaged mitochondrial clearance.
In addition, a PINK1 mutant, which induced mitochondrial enlargement and had been considered as a Drosophila model of Parkinson's disease (PD), caused fly muscle defects, and the loss of vimar could rescue these defects. Furthermore, we found that the mammalian homolog of Vimar, RAP1GDS1 (show RAP1GDS1 Antibodies), played a similar role in regulating mitochondrial morphology, suggesting a functional conservation of this GEF (show SLC2A4RG Antibodies) member.
Buffy has a role enhancing the loss of parkin (show PARK2 Antibodies) and suppressing the loss of Pink1 phenotypes in Drosophila
PINK1-dependent mitophagy suppresses neural neurodegeneration by removing damaged mitochondria.
Clu (show CLU Antibodies) directly modulates mitochondrial function, and that Clu's function contributes to the PINK1-Park pathway of mitochondrial quality control.
Pink1-depleted zebrafish are the first vertebrate model of PINK1 deficiency with loss of dopaminergic neurons.
Our findings suggest that a lack of pink1 in zebrafish alters many vital and critical pathways in addition to the HIF signaling pathway.
Distinct groups of dopaminergic neurons are sensitive to targeted loss of Pink1 factor in a morphant fish model of toxin-induced Parkinson's disease.
Morpholino-mediated loss of pink1 function in zebrafish profoundly affects the development of dopaminergic neurons in the ventral diencephalon and affects behaviour of the zebrafish larvae, namely their response to tactile stimuli and locomotor behavior.
an impaired PINK1-PARK2 (show PARK2 Antibodies)-mediated neuroimmunology pathway contributes to septic death.
We demonstrated that miR (show MLXIP Antibodies)-27a and miR (show MLXIP Antibodies)-27b regulate PINK1 expression and autophagic clearance of damaged mitochondria
The effects of variants in the Parkin (show PARK2 Antibodies), PINK1, and DJ-1 (show PARK7 Antibodies) genes along with evidence for their pathogenicity have been summarized. (Review)
data suggest that ROS (show ROS1 Antibodies) may act as a trigger for the induction of Parkin (show PARK2 Antibodies)/PINK1-dependent mitophagy.
Adipogenic process can be dissected into 3 stages according to the participation of PARL (show PARL Antibodies)-PINK1-Parkin (show PARK2 Antibodies) system. Findings reveal the sequential adipogenic events directed by PARL (show PARL Antibodies)-PINK1-Parkin (show PARK2 Antibodies) system, add more evidence supporting the convergence of pathogenesis leading to neurodegenerative and metabolic disease
PKA-mediated phosphorylation of MIC60 negatively regulates mitochondrial clearance that is initiated by PINK1 and Parkin (show PARK2 Antibodies).
We report that loss of PINK1 contributes to the Warburg effect through ROS (show ROS1 Antibodies)-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.
PINK1 disease mutants failed to recruit synphilin-1 (show SNCAIP Antibodies) and did not activate mitophagy, indicating that PINK1-synphilin-1 (show SNCAIP Antibodies)-SIAH-1 (show SIAH1 Antibodies) represents a new parkin (show PARK2 Antibodies)-independent mitophagy pathway. Drugs that activate this pathway will provide a novel strategy to promote the clearance of damaged mitochondria in Parkinson's disease.
PINK1 p.G411S is a rare genetic risk factor with a relatively large effect size conferred by a partial dominant-negative function phenotype.
In summary, our results demonstrate that PINK1 promoted hepatic IR via JNK (show MAPK8 Antibodies) and ERK (show EPHB2 Antibodies) pathway in PA treated HepG2 cells, implying a novel molecular target for the therapy of diabetes.
study identifies a new role of Dual-AKAP1 (show AKAP1 Antibodies) in regulating mitochondrial trafficking through Miro-2 (show RHOT2 Antibodies), and supports a model in which PINK1 and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Study showed that apoptosis is an important form of cellular degeneration in lipopolysaccharide (LPS (show TLR4 Antibodies)-sensitized hypoxic-ischemic (HI) injury in the immature brain. Loss of PINK1 can protect the immature brain against cell apoptosis induced by LPS (show TLR4 Antibodies)-sensitized HI injury. Moreover, alpha-Syn plays a neuroprotective role in LPS (show TLR4 Antibodies)-sensitized HI brain damage in PINK1-knockout neonatal mice
the results suggest that BNIP3 (show BNIP3 Antibodies) plays a vital role in regulating PINK1 mitochondrial outer membrane localization, the proteolytic process of PINK1 and PINK1/parkin (show PARK2 Antibodies)-mediated mitophagy under physiological conditions.
lack of PINK1 causes increased excitatory transmission and neurotransmitter release in the hippocampus, which might lead to the cognitive decline often observed in Parkinson's disease
The identification of PINK1 and Parkin (show PARK2 Antibodies) as suppressors of an immune-response-eliciting pathway provoked by inflammation suggests new insights into Parkinson's disease pathology.
PINK1 deficiency causes defects in GFAP (show GFAP Antibodies)-positive astrogliogenesis during brain development.
The findings of this study show a CB1R (show CNR1 Antibodies) dysfunction at corticostriatal synapses in PINK1(-/-), but not in PINK1(+/-) mice, and provide a mechanistic link to the distinct plasticity deficits observed in both genotypes.
Loss of PINK1 inhibits Ca2 (show CA2 Antibodies)+ efflux by NCLX (show SLC24A6 Antibodies) and triggers mitochondrial depolarization.
PINK1 gene knockout can protect neonatal mice from hypoxic-ischemic brain damage (HIBD).
This gene encodes a serine/threonine protein kinase that localizes to mitochondria. It is thought to protect cells from stress-induced mitochondrial dysfunction. Mutations in this gene cause one form of autosomal recessive early-onset Parkinson disease.
, PTEN induced putative kinase 1
, PTEN-Induced kinase 1
, PTEN-induced putative kinase 1
, serine/threonine-protein kinase PINK1, mitochondrial
, serine/threonine-protein kinase PINK1, mitochondrial-like
, PTEN-induced putative kinase protein 1
, protein kinase BRPK