PINK1 Antibody [Janelia Fluor® 549]

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Product Details

Summary
Reactivity Hu, Mu, Rt, Dr, RbSpecies Glossary
Applications ICC/IF, IHC, IHC-P
Clonality
Polyclonal
Host
Rabbit
Conjugate
Janelia Fluor 549

PINK1 Antibody [Janelia Fluor® 549] Summary

Immunogen
PINK1 antibody was developed using a synthetic peptide made to the human PINK1 protein sequence (between residues 175-250). [Swiss-Prot Q9BXM7]
Localization
Mitochondrial
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Gene
PINK1
Purity
Immunogen affinity purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Applications/Dilutions

Dilutions
  • Immunocytochemistry/Immunofluorescence
  • Immunohistochemistry
  • Immunohistochemistry-Paraffin
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Reactivity Notes

Drosophila reactivity reported in scientific literature (PMID: 30237395).

Packaging, Storage & Formulations

Storage
Store at 4C in the dark.
Buffer
50mM Sodium Borate
Preservative
0.05% Sodium Azide
Purity
Immunogen affinity purified

Notes

Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.

Alternate Names for PINK1 Antibody [Janelia Fluor® 549]

  • BRPK
  • EC 2.7.11.1
  • FLJ27236
  • PARK6
  • Parkinson disease (autosomal recessive) 6
  • PINK1
  • protein kinase BRPK
  • PTEN induced putative kinase 1
  • PTEN-induced putative kinase protein 1
  • serine/threonine-protein kinase PINK1, mitochondrial

Background

Phosphatase and Tensin Homolog (PTEN) is a tumor suppressor which acts as an antagonist to phosphatidylinositol 3-kinase (PI3K) signaling. PTEN exerts enzymatic activity as a phosphatidylinositol-3,4,5-trisphosphate (PIP3) phosphatase, opposing PI3K activity by reducing availability of PIP3 to proliferating cells. Loss of PTEN function leads to elevated PIP3 and increased activation of PI3K/AKT signaling in many types of cancer.

PINK1 (PTEN induced putative kinase 1) protein contains a N-terminal mitochondrial targeting sequence, putative transmembrane helix, linker region, serine (Ser65)/threonine (Thr257) kinase domain and C-terminal segment. PINK1 is translated in the cytosol, then translocated to the outer mitochondrial membrane where it is rapidly cleaved and degraded as a part of normal mitochondrial function. In damaged (depolarized) mitochondria, PINK1 becomes stabilized and accumulates, resulting in the subsequent phosphorylation of numerous proteins on the mitochondrial surface.

When PINK1 is imported into the cell, mitochondrial processing peptidase, presenilin-associated rhomboid-like protease and AFG3L2 cleave PINK1 and tag it for the ubiquitin-proteasome pathway, keeping low PINK1 protein expression at basal conditions (1,2). Accumulation of PINK1 in mitochondria indicate damage. PINK1 maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (3). PINK1 has a theoretical molecular weight of 63 kDa and undergoes proteolytic processing to generate at least two cleaved forms (55 kDa and 42 kDa).

Ultimately PARK2 (E3 Ubiquitin Ligase Parkin) is recruited to the damaged mitochondria where it is activated by 1) PINK-mediated phosphorylation of PARK2 at serine 65, and 2) PARK2 interaction with phosphorylated ubiquitin (also phosphorylated by PINK1 on serine 65) (4,5). There is a strong interplay between Parkin and PINK1, where loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by Parkin (2,4,5). Mutations in either Parkin or PINK1 alter mitochondrial turnover, resulting in the accumulation of defective mitochondria and, ultimately, neurodegeneration in Parkinson's disease. Mutations in the PINK1 gene located within the PARK6 locus on chromosome 1p35-p36 have been identified in patients with early-onset Parkinson's disease (6).

References

1. Rasool, S., Soya, N., Truong, L., Croteau, N., Lukacs, G. L., & Trempe, J. F. (2018). PINK1 autophosphorylation is required for ubiquitin recognition. EMBO Rep, 19(4). doi:10.15252/embr.201744981

2. Shiba-Fukushima, K., Arano, T., Matsumoto, G., Inoshita, T., Yoshida, S., Ishihama, Y.,... Imai, Y. (2014). Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering. PLoS Genet, 10(12), e1004861. doi:10.1371/journal.pgen.1004861

3. Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L., Kim, J.,... Przedborski, S. (2010). PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc Natl Acad Sci U S A, 107(1), 378-383. doi:10.1073/pnas.0911187107

4. McWilliams, T. G., Barini, E., Pohjolan-Pirhonen, R., Brooks, S. P., Singh, F., Burel, S.,... Muqit, M. M. K. (2018). Phosphorylation of Parkin at serine 65 is essential for its activation in vivo. Open Biol, 8(11). doi:10.1098/rsob.180108

5. Exner, N., Treske, B., Paquet, D., Holmstrom, K., Schiesling, C., Gispert, S.,... Haass, C. (2007). Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci, 27(45), 12413-12418. doi:10.1523/jneurosci.0719-07.2007

6. Valente, E. M., Bentivoglio, A. R., Dixon, P. H., Ferraris, A., Ialongo, T., Frontali, M.,... Wood, N. W. (2001). Localization of a novel locus for autosomal recessive early-onset parkinsonism, PARK6, on human chromosome 1p35-p36. Am J Hum Genet, 68(4), 895-900. doi:10.1086/319522

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Product General Protocols

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Video Protocols

ICC/IF Video Protocol

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Secondary Antibodies

 

Isotype Controls

Other Available Formats

Alexa Fluor 350 BC100-494AF350
Alexa Fluor 405 BC100-494AF405
Alexa Fluor 488 BC100-494AF488
Alexa Fluor 594 BC100-494AF594
Alexa Fluor 647 BC100-494AF647
Alexa Fluor 700 BC100-494AF700
Alexa Fluor 750 BC100-494AF750
Biotin BC100-494B
DyLight 350 BC100-494UV
DyLight 405 BC100-494V
DyLight 488 BC100-494G
DyLight 550 BC100-494R
DyLight 594 BC100-494DL594
DyLight 650 BC100-494C
DyLight 680 BC100-494FR
DyLight 755 BC100-494IR
FITC BC100-494F
HRP BC100-494H
Janelia Fluor 549 BC100-494JF549
Janelia Fluor 646 BC100-494JF646

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Blogs on PINK1. Showing 1-10 of 12 blog posts - Show all blog posts.

Losing memory: Toxicity from mutant APP and amyloid beta explain the hippocampal neuronal damage in Alzheimer's disease
By Jamshed Arslan Pharm.D. Alzheimer's disease (AD) is an irreversible brain disorder that destroys memory and thinking skills. The telltale signs of AD brains are extracellular deposits of amyloid beta (a polypepti...  Read full blog post.

There's an autophagy for that!
By Christina Towers, PhDA critical mechanism that cells use to generate nutrients and fuel metabolism is through a process called autophagy.  This process is complex and involves over 20 different proteins, most of which are highly conserved acro...  Read full blog post.

The role of Parkin and autophagy in retinal pigment epithelial cell (RPE) degradation
The root of Parkinson’s disease (PD) points to a poorly regulated electron transport chain leading to mitochondrial damage, where many proteins need to work cohesively to ensure proper function.  The two key players of this pathway are PINK1,...  Read full blog post.

The identification of dopaminergic neurons using Tyrosine Hydroxylase in Parkinson's research and LRRK2
Tyrosine hydroxylase (TH) is a crucial enzyme involved in the biosynthesis of dopamine, norepinephrine and epinephrine in the brain.  Specifically, TH catalyzes the conversion of l-tyrosine to l-dihydroxyphenylalanine (l-dopa).  The importance of t...  Read full blog post.

Parkin - Role in Mitochondrial Quality Control and Parkinson's Disease
Parkin/PARK2 is a cytosolic enzyme which gets recruited to cellular mitochondria damaged through depolarization, ROS or unfolded proteins accumulation, and exert protective effects by inducing mitophagy (mitochondrial autophagy). Parkin induces mit...  Read full blog post.

PINK1 - performing mitochondrial quality control and protecting against Parkinson’s disease
PTEN-induced putative kinase 1 (PINK1) is a serine/threonine kinase with important functions in mitochondrial quality control. Together with the Parkin protein, PINK1 is able to regulate the selective degradation of damaged mitochondria through aut...  Read full blog post.

PINK1: All work and no fun
The protein PINK1 is a mitochondrial-located serine/threonine kinase (PTK) that maintains organelle function and integrity. It not only protects organelles from cellular stress, but it also uses the selective auto-phagocytosis process for cleaning and...  Read full blog post.

PINK1 and its role in Parkinson's disease
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 mitochondr...  Read full blog post.

PINK1: Promoting Organelle Stability and Preventing Parkinson's disease
PINK1 is a protein serine/threonine kinase (PTK) that protects the organelles from cellular stress and controls selective autophagy to clear damage. Exner, et al. were among the first to report that PINK1 deficiency in humans was linked to autosomal r...  Read full blog post.

PINK1: Promoting Organelle Stability and Preventing Parkinson's disease
PINK1 is a protein serine/threonine kinase (PTK) that protects the organelles from cellular stress and controls selective autophagy to clear damage. Exner, et. al. were among the first to report that PINK1 deficiency in humans was linked to autosomal...  Read full blog post.

Showing 1-10 of 12 blog posts - Show all blog posts.

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Bioinformatics

Gene Symbol PINK1