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Phospho-Ser378 Parkin Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | O60260 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 52 KDa |
| Gene ID | 5071 |
|---|---|
| Gene Name | PARK2 |
| Other Names | E3 ubiquitin-protein ligase parkin, 632-, Parkinson juvenile disease protein 2, Parkinson disease protein 2, PARK2, PRKN |
| Target/Specificity | Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser378 conjugated to KLH. |
| Dilution | WB~~ 1:1000 |
| Format | Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns. |
| Antibody Specificity | Specific for the ~52k parkin protein phosphorylated at Ser378. Immunolabeling of the parkin band is absent in parkin S378 mutants. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Phospho-Ser378 Parkin Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
Parkin is an E3 ligase in the ubiquitin-proteasome system. Hereditary Parkinson’s disease is most commonly caused by mutations in the parkin gene and is characterized by the progressive loss of dopaminergic neurons and the presence of Lewy bodies in the substania nigra (Jenner et al.,1992). Recent evidence suggests that phosphorylation of parkin at Ser378 may have an important regulatory role on its E3 ubiquitin ligase activity (Yamamoto et al., 2005).
References
Jenner P, Dexter DT, Sian J, Schapira AH, Marsden CD (1992) Oxidative stress as a cause of nigral cell death in Parkinson’s disease and incidental Lewy body disease. Ann Neurol. 32 Suppl: S82-7.
Yamamoto A, Friedlein A, Imai Y, Takahashi R, Kahle PJ, Haass C (2005) Parkin phosphorylation and modulation of its E# ubiquitin ligase activity. J Biol chem. 280(5):3390-9
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