|Other Names||Synphilin-1, Sph1, Alpha-synuclein-interacting protein, SNCAIP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6411a was selected from the SNCAIP region of human Synphilin-1 (SNCAIP). A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1.|
|Cellular Location||Cytoplasm. Note=Detected in cytoplasmic inclusion bodies, together with SNCA|
|Tissue Location||Detected in brain (at protein level). Widely expressed, with highest levels in brain, heart and placenta|
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Parkinson is the second most common neurodegenerative disease after Alzheimers. About 1 percent of people over the age of 65 and 3 percent of people over the age of 75 are affected by the disease. The mutation is the most common cause of Parkinson disease identified to date. Synuclein alpha interacting protein (Synphilin-1) contains several protein-protein interaction domains and interacts with alpha synuclein in neurons. Mutations of SNCAIP have been linked to Parkinson disease. The amino acid sequence of synphilin-1 shows extensive homology with its human counterpart, especially in regions containing ankyrin-like motifs and the coiled-coil domain. Expression of mouse synphilin-1 in tissues is similar to its human counterpart. Synphilin-1 has an important role in the formation of aggregates and cytotoxicity in Parkinson disease and that Dorfin may be involved in the pathogenic process by ubiquitylation of synphilin-1. Role of synphilin-1 in synaptic function and protein degradation and in the molecular mechanisms leading to neurodegeneration in Parkinson disease
Kruger,R. Cell Tissue Res. 318 (1), 195-199 (2004)Lee,G., etal. J. Biol. Chem. 279 (8), 6834-6839 (2004)Tanaka,M., et al. J. Biol. Chem. 279 (6), 4625-4631 (2004)Nagano,Y., et al. J. Biol. Chem. 278 (51), 51504-51514 (2003)Marx,F.P., etal. Hum. Mol. Genet. 12 (11), 1223-1231 (2003)Junn,E., et al. J. Biol. Chem. 277 (49), 47870-47877 (2002)Chung,K.K., et al. Nat. Med. 7 (10), 1144-1150 (2001)Kawamata,H., et al. J. Neurochem. 77 (3), 929-934 (2001)Engelender,S., et al. Nat. Genet. 22 (1), 110-114 (1999)
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