Rabbit anti-Human, Mouse PINK1 Polyclonal Antibody | anti-PINK1 antibody
PINK1, CT (PARK6, Serine/threonine-protein kinase PINK1, mitochondrial, BRPK, PTEN-induced putative kinase protein 1) (MaxLight 650)
NCBI and Uniprot Product Information
NCBI Description
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. [provided by RefSeq, Jul 2008]
Uniprot Description
PINK1: Protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). It is necessary for PARK2 recruitment to dysfunctional mitochondria to initiate their degradation. Interats with PARK2. 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. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Kinase, protein; Membrane protein, integral; Protein kinase, Ser/Thr (non-receptor); Mitochondrial; EC 2.7.11.1; Protein kinase, Other; Other group; NKF2 family
Chromosomal Location of Human Ortholog: 1p36
Cellular Component: mitochondrion; mitochondrial intermembrane space; cytosol; mitochondrial outer membrane; cytoskeleton; membrane; axon; perinuclear region of cytoplasm; cytoplasm; mitochondrial inner membrane; TORC2 complex; chromatin; nucleus; integral to mitochondrial outer membrane
Molecular Function: protein kinase B binding; protein serine/threonine kinase activity; protein binding; protease activator activity; protease binding; ubiquitin protein ligase binding; magnesium ion binding; kinase activity; ATP binding
Biological Process: ubiquitin-dependent protein catabolic process; negative regulation of JNK cascade; positive regulation of dopamine secretion; positive regulation of translation; regulation of protein ubiquitination; protein ubiquitination; protein amino acid phosphorylation; positive regulation of protein amino acid dephosphorylation; negative regulation of macroautophagy; regulation of mitochondrial membrane potential; positive regulation of ubiquitin-protein ligase activity; response to stress; regulation of protein complex assembly; negative regulation of neuron apoptosis; regulation of hydrogen peroxide metabolic process; mitochondrion organization and biogenesis; positive regulation of I-kappaB kinase/NF-kappaB cascade; protein stabilization; activation of protein kinase B; positive regulation of synaptic transmission, dopaminergic; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; peptidyl-serine phosphorylation; mitochondrion degradation; positive regulation of transcription factor activity; positive regulation of protein amino acid phosphorylation; response to oxidative stress; phosphorylation
Disease: Parkinson Disease 6, Autosomal Recessive Early-onset
Research Articles on PINK1
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