Serine/threonine-protein kinase PINK1; mitochondrial; BRPK; PTEN-induced putative kinase protein 1; Pink1

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

Polyclonal

Rabbit Ig

Rabbit

This Mouse Pink1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 118-146 amino acids from the N-terminal region of mouse Pink1.

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.5 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

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 protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins (By similarity).

Cardiovascular; Neuroscience; Signal Transduction

Western Blot (WB), ELISA (EIA)

WB~~1:1000

Mouse Pink1 Antibody (N-term) western blot analysis in mouse heart tissue lysates (35ug/lane).This demonstrates the Pink1 antibody detected the Pink1 protein (arrow).

63181

PTEN induced putative kinase 1

serine/threonine-protein kinase PINK1, mitochondrial

Serine/threonine-protein kinase PINK1, mitochondrial

PINK1_MOUSE

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: Mitochondrial; Protein kinase, Other; Protein kinase, Ser/Thr (non-receptor); Kinase, protein; Membrane protein, integral; EC 2.7.11.1; Other group; NKF2 family

Cellular Component: mitochondrion; integral to membrane; 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: transferase activity; protein kinase B binding; protein serine/threonine kinase activity; protease binding; metal ion binding; ubiquitin protein ligase binding; transferase activity, transferring phosphorus-containing groups; magnesium ion binding; nucleotide binding; kinase activity; ATP binding; protein kinase activity

Biological Process: 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; regulation of neuron apoptosis; regulation of protein complex assembly; response to stress; 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; positive regulation of synaptic transmission, dopaminergic; positive regulation of peptidyl-serine phosphorylation; peptidyl-serine phosphorylation; mitochondrion degradation; autophagy; positive regulation of catecholamine secretion; positive regulation of transcription factor activity; positive regulation of protein amino acid phosphorylation; response to oxidative stress; phosphorylation

Matsuda, N., et al. J. Cell Biol. 189(2):211-221(2010)
Kawajiri, S., et al. FEBS Lett. 584(6):1073-1079(2010)
Kim, K.H., et al. Neurosci. Lett. 468(3):272-276(2010)
Morais, V.A., et al. EMBO Mol Med 1(2):99-111(2009)
Chiba, M., et al. Cytogenet. Genome Res. 126(3):259-270(2009)

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