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

Monoclonal

IgG1

Mouse

This antibody recognizes human, mouse, and rat PINK1.

100ug (1mg/ml) Protein G-purified antibody in PBS, pH 7.4, 0.1% sodium azide, 50% glycerol.

This product is stable for at least one (1) year 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 that maintains mitochondrial function and integrity, provides protection against mitochondrial dysfunction during cellular stress, and is involved in the clearance of damaged mitochondria via selective autophagy. PINK1 is synthesized as a 63kDa protein which undergoes proteolytic processing to yield two cleaved forms, ~55kDa and ~42kDa. PINK1 may be localized to the outer mitochondrial membrane with its kinase domain facing the cytosol which would explain the observed physical interaction between PINK1 and cytosolic E3 ubiquitin ligase Parkin.

Immunoblot, Immunofluorescence (IF)

Immunoblot: 1-5ug/ml. A band of ~50kDa is detected.
IF: 10ug/ml
Dilute in PBS or medium that is identical to that used in the assay system.

Detection of PINK1 in 15ug rat brain lysate at 5ug/ml.

Detection of PINK1 is neuroblastoma cell line SKN-BE at 10ug/ml: DAPI (blue) nuclear stain, Texas RedF actin stain, FITC (green) PINK1 stain.

30,104 Da

PTEN induced kinase 1

serine/threonine-protein kinase PINK1, mitochondrial

Serine/threonine-protein kinase PINK1, mitochondrial

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]

Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN (PubMed:14607334, PubMed:15087508, PubMed:19229105, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:23620051, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:24896179, PubMed:25527291). Targets PRKN to dysfunctional depolarized mitochondria through the phosphorylation of MFN2 (PubMed:23620051). Activates PRKN in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and (2) mediating phosphorylation of ubiquitin, converting PRKN to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 ().

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