PINK1 293T Cell Transient Overexpression Lysate
Novus Biologicals, part of Bio-Techne | Catalog # H00065018-T02
Key Product Details
Species
Human
Applications
SDS-PAGE, Western Blot
Product Summary for PINK1 293T Cell Transient Overexpression Lysate
Quality control test: Transient overexpression cell lysate was tested with Anti-PINK1 antibody by Western Blots. Plasmid: pCMV-PINK1 full-length
Product Specifications
Specificity
PINK1 293T Cell Transient Overexpression Lysate(Denatured)
TMW
62.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Type
293T Cell Transient Overexpression
Protein State
Denatured
Scientific Data Images for PINK1 293T Cell Transient Overexpression Lysate
![Western Blot: PINK1 293T Cell Transient Overexpression Lysate [H00065018-T02]](https://resources.bio-techne.com/images/products/PINK1-Overexpression-Lysate-Denatured-Western-Blot-H00065018-T02-img0003.jpg "Western Blot: PINK1 293T Cell Transient Overexpression Lysate [H00065018-T02]")
Western Blot: PINK1 293T Cell Transient Overexpression Lysate [H00065018-T02]
Western Blot: PINK1 Overexpression Lysate (Denatured) [H00065018-T02] - Lane 1: PINK1 transfected lysate, obseved molecular weight at 62.70 KDaLane 2: Non-transfected lysate.
Formulation, Preparation, and Storage
Formulation
1X Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2-mercaptoethanol, 0.01% Bromophenol blue)
Concentration
mg/ml
Shipping
The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Storage
Store at -80C. Avoid freeze-thaw cycles.
Background: PINK1
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
Long Name
PTEN-induced Putative Kinase 1
Alternate Names
BRPK, PARK6
Gene Symbol
PINK1
Additional PINK1 Products
Product Documents for PINK1 293T Cell Transient Overexpression Lysate
Product Specific Notices for PINK1 293T Cell Transient Overexpression Lysate
This product is produced by and distributed for Abnova, a company based in Taiwan.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Lysates are guaranteed for 6 months from date of receipt.
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