PINK1 Human; PTEN Induced Putative Kinase 1 Human Recombinant; PTEN induced putative kinase 1; PARK6; protein kinase BRPK; Parkinson disease (autosomal recessive) 6; serine/threonine-protein kinase PINK1 mitochondrial; EC 2.7.11.1

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

E Coli

Greater than 90% as determined by SDS-PAGE.

The PINK1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.
Sterile Filtered colorless solution.

Small volumes of PINK1 recombinant protein 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.

Description: PINK1 Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (156-507) and having a molecular mass of 37.9 kDa.PINK1 is purified by proprietary chromatographic techniques.

Introduction: PINK1 is a serine/threonine protein kinase which is found in the mitochondria. PINK1 shields cells from stress-induced mitochondrial dysfunction. Mutations results in one form of autosomal recessive early-onset Parkinson disease.

PROTEIN KINASES; Enzymes; Protein Kinases

30,104 Da

PTEN induced putative kinase 1

serine/threonine-protein kinase PINK1, mitochondrial; PTEN-induced putative kinase protein 1; protein kinase BRPK

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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