PINK1, Monoclonal Antibody

Mouse Anti-Human PINK1 Monoclonal IgG1; PINK1 Antibody: Dylight 488; Parkinson disease (autosomal recessive) 6 Antibody; EC 2.7.11.1 Antibody; PARK6 Antibody; serine/threonine-protein kinase PINK1 mitochondrial Antibody; PTEN-induced putative kinase protein 1 Antibody; protein kinase BRPK Antibody; BRPK Antibody; FLJ27236 Antibody; PTEN induced putative kinase 1 Antibody; Phosphatase and Tensin Homolog Antibody

For Research Use Only. Not for use in diagnostic procedures.

Monoclonal

IgG1

S4-15

Mouse

Detects ~50 kDa.

Protein G Purified

PBS pH 7.4, 50% Glycerol, 0.1% Sodium Azide

1 mg/ml (lot specific)

Store at-20 degree C.

Small volumes of anti-PINK1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

PINK1 (PTEN induced putative kinase 1) is a mitochondrial serine/threonine kinase which maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). PINK1 is synthesized as a 63 kD protein which undergoes proteolyt processing to generate at least two cleaved forms (55 kD and 42 kD). PINK1 and its substrates have been found in the cytosol as well as in different sub-mitochondrial compartments, and according to the recent reports; PINK1 may be targeted to OMM (outer mitochondrial membrane) with its kinase domain facing the cytosol, providing a possible explanation for the observed physical interaction with the cytosolic E3 ubiquitin ligase Parkin. Defective PINK1 may cause alterations in processing, stability, localization and activity as well as binding to substrates/interaction-partners which ultimately leads to differential effects on mitochondrial function and morphology. Mutations in PINK1 are linked to autosomal recessive early onset Parkinson's disease, and are associated with loss of protective function, mitochondrial dysfunction, aggregation of alpha-synuclein, as well as proteasome dysfunction.

Neuroscience; Cell Signaling; Post-Translational Modifications; Phosphorylation; Cardiovascular System; Heart

Western Blot (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)

WB: 1:1000

Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-PINK1 Monoclonal Antibody, Clone S4-15 at 1:100 for 60 min at RT. Secondary Antibody: Goat Anti-Mouse ATTO 488 at 1:100 for 60 min at RT. Counterstain: Phalloidin Texas Red F-Actin stain; DAPI (blue) nuclear stain at 1:1000; 1:5000 for 60 min RT, 5 min RT. Localization: Cytoplasm. Magnification: 60X. (A) DAPI (blue) nuclear stain. (B) Phalloidin Texas Red F-Actin stain. (C) PINK1 Antibody. (D) Composite.

Western Blot analysis of Rat Brain showing detection of ~50 kDa PINK1 protein using Mouse Anti-PINK1 Monoclonal Antibody, Clone S4-15 at 1:200 for 16 hours at 4 degree C. Secondary Antibody: Goat Anti-Mouse IgG: HRP at 1:1000 for 1 hour RT. Color Development: ECL solution for 6 min in RT. Predicted/Observed Size: ~50 kDa.

PTEN induced kinase 1

serine/threonine-protein kinase PINK1, mitochondrial

Serine/threonine-protein kinase PINK1, mitochondrial

PINK1_HUMAN

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]

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

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