Synuclein, alpha Interacting Protein (SNCAIP) (C-Term) antibody

Antigen: Synuclein, alpha Interacting Protein (SNCAIP)

Synonyms: SYPH1, MGC39814, Syph1, sncaip, MGC88953, SNCAIP, LOC100221074

Epitope: C-Term

Clonality: Polyclonal

Host: Rabbit

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350929

Additional Information

Alternative name: Synphilin-1 (Synphilin 1,alpha synuclein interacting protein) (c-terminal region)

Swiss-Prot: Q9Y6H5

Immunogen: A synthetic peptide from the c-terminal of human Synphilin-1 (Synphilin 1, alpha synuclein interacting protein) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen shares 83% identity with mouse sequence.

Format: Lyophilized

Description: Tissue specificity: Widely expressed, with highest levels in brain, heart and placenta. Defects in SNCAIP are a cause of Parkinson disease (PD). PD is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. Constructs encoding portions of SNCA and SNCAIP co-transfected in mammalian cells promote cytosolic inclusions resembling the Lewy bodies of Parkinson disease. Coexpression of SNCA, SNCAIP, and PARK2 result in the formation of Lewy body-like ubiquitin-positive cytosolic inclusions. Familial mutations in PARK2 disrupt the ubiquitination of SNCAIP and the formation of the ubiquitin-positive inclusions. These results provide a molecular basis for the ubiquitination of Lewy body-associated proteins and link PARK2 and SNCA in a common pathogenic mechanism through their interaction with SNCAIP. Also known as: Alpha-synuclein-interacting protein, SNCAIP.

Specificity: Appears to be specific for Synphilin-1.

Application Details

Application Notes: IHC, WB. A dilution of 1: 300 to 1: 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.

Purity: whole serum

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Publications

Publications: Engelender, Wanner, Kleiderlein et al.: "Organization of the human synphilin-1 gene, a candidate for Parkinson's disease." in: Mammalian genome : official journal of the International Mammalian Genome Society, Vol. 11, Issue 9, pp. 763-6, 2000 (PubMed).

Chung, Zhang, Lim et al.: "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease." in: Nature medicine, Vol. 7, Issue 10, pp. 1144-50, 2001 (PubMed).

Ito, Niwa, Hishikawa et al.: "Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1." in: The Journal of biological chemistry, Vol. 278, Issue 31, pp. 29106-14, 2003 (PubMed).

Nagano, Yamashita, Takahashi et al.: "Siah-1 facilitates ubiquitination and degradation of synphilin-1." in: The Journal of biological chemistry, Vol. 278, Issue 51, pp. 51504-14, 2003 (PubMed).

Imami, Sugiyama, Kyono et al.: "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." in: Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, Vol. 24, Issue 1, pp. 161-6, 2008 (PubMed).