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PINK1 truncated Antibody (600-401-GU5) in ICC/IF
Immunofluorescence Microscopy of Rabbit anti-PINK1 truncated antibody. Cell line: NIH 3T3 (p/n W10-000-358). Fixation: 0.5% PFA. Antigen retrieval: not required. Primary antibody: PINK1 truncated antibody at 20 µg/mL for overnight at 4°C. Secondary antibody: Anti-RABBIT IgG DyLight™ 488 Conjugated Preadsorbed (p/n 611-741-127) at 5 µg/mL for 2 hrs at RT. Localization: PINK1 is mitochondrial and cytoplasmic.... View More
Product Details
600-401-GU5
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human,
Mouse
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
Anti-PINK1 truncated antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to a C-Term portion of human PINK1 conjugated to Keyhole Limpet Hemocyanin (KLH).
Conjugate
Form
Liquid
Concentration
1 mg/mL
Purification
Affinity chromatography
Storage buffer
0.02M potassium phosphate, pH 7.2, with 0.15M NaCl
Contains
0.01% sodium azide
Storage conditions
-20° C, Avoid Freeze/Thaw Cycles
Shipping conditions
Wet ice
Product Specific Information
Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
This affinity purified antibody is directed against human PINK1. Blast analysis of the sequence of the immunogen shows 100% identity with human and 93% identity to mouse.
Target Information
PINK1 (PTEN-induced putative kinase 1) protects from mitochondrial dysfunction in cells by conferring different autophosphorylation activity to mitochondrial genes. The kinase domain of PINK1 appears to be critical in its protective effects. Mitochondrial proteins are critical for the regulation of cellular energy and adaptation to stress. Particularly in brain cells, mitochondrial demand is extraordinarily high, in order to accommodate aerobic and anaerobic support of high energy processes. When mitochondrial structure and/or function is disrupted in the brain, neurodegenerative diseases like Parkinson's disease are triggered.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: BRPK; FLJ27236; PINK 1; PINK-1; protein kinase BRPK; PTEN-induced putative kinase protein 1; Serine/threonine-protein kinase PINK1, mitochondrial
Gene Aliases: 1190006F07Rik; AU042772; AW557854; BRPK; mFLJ00387; PARK6; PINK1
UniProt ID: (Human) Q9BXM7, (Mouse) Q99MQ3
Entrez Gene ID: (Human) 65018, (Mouse) 68943
magnesium ion binding
protease binding
protein kinase activity
protein serine/threonine kinase activity
protein binding
ATP binding
calcium-dependent protein kinase activity
kinase activity
peptidase activator activity
ubiquitin protein ligase binding
protein kinase B binding
C3HC4-type RING finger domain binding
nucleotide binding
transferase activity
transferase activity, transferring phosphorus-containing groups
metal ion binding
non-receptor serine/threonine protein kinase
protein modifying enzyme
mitophagy
positive regulation of protein phosphorylation
regulation of oxidative phosphorylation
protein phosphorylation
ubiquitin-dependent protein catabolic process
response to stress
response to oxidative stress
mitochondrion organization
regulation of hydrogen peroxide metabolic process
negative regulation of gene expression
regulation of mitochondrion organization
positive regulation of peptidase activity
macroautophagy
positive regulation of macroautophagy
negative regulation of macroautophagy
phosphorylation
protein ubiquitination
peptidyl-serine phosphorylation
respiratory electron transport chain
regulation of protein ubiquitination
positive regulation of protein ubiquitination
activation of protein kinase B activity
positive regulation of synaptic transmission, dopaminergic
positive regulation of peptidyl-serine phosphorylation
positive regulation of dopamine secretion
cellular response to oxidative stress
positive regulation of protein dephosphorylation
intracellular signal transduction
peptidyl-serine autophosphorylation
TORC2 signaling
positive regulation of I-kappaB kinase/NF-kappaB signaling
regulation of protein complex assembly
negative regulation of neuron apoptotic process
positive regulation of translation
negative regulation of JNK cascade
protein stabilization
positive regulation of sequence-specific DNA binding transcription factor activity
positive regulation of ubiquitin-protein transferase activity
regulation of mitochondrial membrane potential
positive regulation of protein kinase B signaling
regulation of proteasomal protein catabolic process
cellular response to hypoxia
establishment of protein localization to mitochondrion
maintenance of protein location in mitochondrion
positive regulation of mitochondrial fission
positive regulation of release of cytochrome c from mitochondria
negative regulation of mitochondrial fission
cellular response to toxic substance
mitophagy in response to mitochondrial depolarization
regulation of synaptic vesicle transport
negative regulation of autophagosome assembly
positive regulation of mitochondrial electron transport, NADH to ubiquinone
regulation of mitophagy
negative regulation of mitophagy
negative regulation of oxidative stress-induced cell death
negative regulation of oxidative stress-induced neuron death
regulation of protein targeting to mitochondrion
negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway
negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
positive regulation of cristae formation
positive regulation of protein targeting to mitochondrion
positive regulation of free ubiquitin chain polymerization
regulation of reactive oxygen species metabolic process
negative regulation of reactive oxygen species metabolic process
positive regulation of ATP biosynthetic process
autophagy
positive regulation of catecholamine secretion
regulation of neuron apoptotic process
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
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