- Peptide (C)KELHHFRILGEEQYTR, corresponding to amino acid residues 298 - 313 of mouse Parkin (Accession Q9WVS6). Intracellular.
- Western blot analysis of rat brain synaptosome preparation (lanes 1 and 3) and mouse brain lysates (lanes 2 and 4):1-2. Anti-Parkin Antibody (#ANR-103), (1:200).
3-4. Anti-Parkin Antibody, preincubated with Parkin Blocking Peptide (BLP-NR103).
- Western blot analysis of human SH-SY5Y neuroblastoma cell line lysate:1. Anti-Parkin Antibody (#ANR-103), (1:200).
2. Anti-Parkin Antibody, preincubated with Parkin Blocking Peptide (BLP-NR103).
- Expression of Parkin in rat brain 4th ventricle.Immunohistochemical staining of perfusion-fixed frozen rat brain sections with Anti-Parkin Antibody (#ANR-103), (1:200), followed by goat Anti-rabbit-AlexaFluor-488. A. Parkin immunoreactivity (green) appears along the wall of the 4th cerebral ventricle (arrows). B. Pre-incubation of the antibody with Parkin Blocking Peptide (BLP-NR103), suppressed staining. Cell nuclei are stained with DAPI (blue). 4th V= 4th ventricle.
- Pohl, C. et al. (2019) Science., 366, 818.
- Hoeller, D. et al. (2016) Proc. Natl. Acad. Sci., 113, 13266.
- Panicker, N. et al. (2017) Boichem. J., 474, 3075.
- Murillo-González, F.E. et al. (2021) Biochem. Pharmacol., 190, 114650.
- George, J.A. et al. (2018) Front. Genet., 9,29.
Protein degradation is a major process in the cell, allowing control and adjustment of the levels of proteins. The enzyme responsible for the vast majority of cellular protein degradation is the 26S proteasome1. Protein degradation is a highly regulated process that dependents on specific poly-ubiquitination of the substrate. The ubiquitination pathway is catalyzed by E1, E2 and E3 enzymes that activate, conjugate, and ligate, respectively, the ubiquitin protein to the substrate protein2.
Parkin is a cytosolic E3 ubiquitin ligase that plays an important role in neuroprotection. Structurally, the Parkin protein is comprised of a ubiquitin-like (Ubl) domain at its N-terminus and a really interesting new gene (RING)1–in-between-ring (IBR) –RING2 domain and a zinc-chelating (RING0) domain at its C-terminus. E2 ubiquitin-conjugated enzymes are recruited to the RING1 domain where they transfer ubiquitin to the RING2 domain at the Parkin catalytic site. The ubiquitin is then transferred to the substrate protein, where it serves as a tag for recognition by the proteasome3.
Parkin activity prevent the accumulation and aggregation of damaged proteins and therefore it protects against unfolded protein stress. In addition, it is known to promote the elimination of aberrant mitochondria via mitophagy4. Mutations in Parkin have been associated with Parkinson’s disease (PD), Alzheimer’s disease and Huntington’s disease5.
Species reactivity key:
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Anti-Parkin Antibody (#ANR-103) is a highly specific antibody directed against an epitope of the mouse protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize Parkin from rat, mouse and human samples.