PINK1 Antibody (8E10.1D6) - BSA Free

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

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.

We have publications tested in 3 confirmed species: Human, Mouse, Rat.

We have publications tested in 3 applications: ICC/IF, IHC-P, WB.

Showing Publications 1 - 10 of 10.

Publications using NBP2-36488	Applications	Species
Roberta Tufi, Emily H Clark, Tamaki Hoshikawa, Christiana Tsagkaraki, Jack Stanley, Kunitoshi Takeda, James M Staddon, Thomas Briston High-content phenotypic screen to identify small molecule enhancers of Parkin-dependent ubiquitination and mitophagy. SLAS discovery : advancing life sciences R & D 2023-04-25 [PMID: 36608804]
Di Rienzo M, Romagnoli A, Ciccosanti F Et al. AMBRA1 regulates mitophagy by interacting with ATAD3A and promoting PINK1 stability Autophagy 2021-11-19 [PMID: 34798798] (ICC/IF, WB, Human)	ICC/IF, WB	Human
Meng Q, Zaharieva EK, Sasatani M, Kobayashi J. Possible relationship between mitochondrial changes and oxidative stress under low dose-rate irradiation Redox Report 2021-08-26 [PMID: 34435550]
Shin N, Shin HJ, Yi Y et al. p66shc siRNA-Encapsulated PLGA Nanoparticles Ameliorate Neuropathic Pain Following Spinal Nerve Ligation Polymers (Basel) 2020-04-29 [PMID: 32365512] (WB, Rat)	WB	Rat
Han H, Chou CC, Li R et al. Chalcomoracin is a potent anticancer agent acting through triggering Oxidative stress via a mitophagy- and paraptosis-dependent mechanism Sci Rep 2018-06-22 [PMID: 29934599] (WB, Human)	WB	Human
Piao Y, Gwon DH, Kang DW et al. TLR4-mediated autophagic impairment contributes to neuropathic pain in chronic constriction injury mice. Mol Brain. 2018-02-27 [PMID: 29486776] (IHC-P, Mouse) Details: Mouse monoclonal PINK1 antibody from Novus was used to examine differences in expression of PINK 1 IR cells in the ipsilateral and contralateral side in WT mice vs TLR4 KO mice	IHC-P	Mouse
Kim MJ, Hwang JW, Yun CK, Lee Y. Delivery of exogenous mitochondria via centrifugation enhances cellular metabolic function. Sci Rep. 2018-02-20 [PMID: 29463809] (WB, Human)	WB	Human
Tan WJT, Song L, Li Y et al. Novel Role of the Mitochondrial Protein Fus1 in Protection from Premature Hearing Loss via Regulation of Oxidative Stress and Nutrient and Energy Sensing Pathways in the Inner Ear Antioxid Redox Signal. 2017-09-09 [PMID: 28135838] (WB, Mouse)	WB	Mouse
Juyeon K, Park JH, Park YS, Koh HC. PPAR-gamma activation attenuates deltamethrin-induced apoptosis by regulating cytosolic PINK1 and inhibiting mitochondrial dysfunction. Toxicol. Lett. 2016-08-20 [PMID: 27553674]
Greene A W, Grenier K et al. Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. EMBO Rep 2012-01-04 [PMID: 22354088] (WB, Human)	WB	Human

Array NBP2-36488

• PINK1 Antibodies
• PINK1 Lysates
• PINK1 Proteins
• PINK1 Proteins and Enzyme