Recombinant Human His6-Parkin, CF

Recombinant Human His6-Parkin, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Parkin

Parkin, also known as Parkinson Juvenile Disease Protein 2, is a 465 amino acid (aa), cytoplasmic and mitochondrial enzyme with a predicted molecular weight of 51.5 kDa, that functions as a RING-type Ubiquitin ligase (E3) (1,2). Human Parkin shares 75% and 78% aa sequence identity with mouse and rat Parkin, respectively. Human Parkin2 lacks exon 5 which encodes aa 179-206 of Parkin. The structure of Parkin includes an N-terminal Ubiquitin-like motif and a C-terminal RING domain composed of two RING finger motifs separated by two IBR domains. Parkin functions in conjunction with the Ubiquitin-conjugating (E2) enzymes UbcH7, UbcH8, and Ubc13/Uev1 (1,4,5). Together with PTEN-induced Putative Kinase 1 (PINK1), Parkin is important for maintaining functional mitochondria (5). Parkin is recruited to dysfunctional mitochondria in a PINK1-dependent manner, where it ubiquitinates outer mitochondrial proteins and drives autophagic degradation (6,7). Parkin is expressed in heart, testis, and skeletal muscle but is detected at the highest levels in brain. Mitochondrial dysfunction is thought to be central to the pathogenesis of Parkinson's disease (PD). This hypothesis is supported by the fact that mutations in Parkin and PINK1 result in recessive forms of the disease (8). Parkin is also thought to exert neuroprotective effects via regulation of the unfolded-protein stress response and targeting of various substrates for proteasomal degradation (9). Mutations in Parkin often affect E3 ligase activity through decreased E2 and/or substrate interactions, which result in the dysfunction of proteasomal degradation pathways and the neurotoxic accumulation of misfolded proteins (10).

Parkin can auto-ubiquitinate itself and ubiquitinate various substrates (eg. CDCrel-1 and Rel-2a, Cyclin E, Synphilin-1, the O-glycosylated form of alpha -Synuclein ( alpha Sp22), PAel-R,FBP1, alpha / beta Tubulin, RanBP2, Hsp70, Synaptotagmin XI) in an E2-dependent manner, targeting them for degradation. This protein contains a N-terminal His6-tag.

Related Research Areas

• E3 Ubiquitin Ligases
• Neurodegenerative Disease
• Parkinson's Disease Related Molecules
• Search Ubiquitin-related Enzymes
• Ubiquitin-related Molecules in the Akt Pathway