The SNCAIP Polyclonal Antibody (PAC052918) is a crucial tool for researchers studying the role of SNCAIP in neurodegenerative diseases like Parkinson's disease. SNCAIP, also known as alpha-synuclein interacting protein, is involved in the pathogenesis of Parkinson's disease through its interaction with alpha-synuclein, a key player in the formation of Lewy bodies.This antibody, raised in rabbits, is highly specific to human samples and has been validated for use in immunohistochemistry and western blot applications. By binding to SNCAIP, the antibody allows for the detection and analysis of this protein in various cell types and tissues, making it an essential tool for studies focused on understanding the molecular mechanisms underlying Parkinson's disease.
The role of SNCAIP in regulating alpha-synuclein levels and toxicity highlights its potential as a therapeutic target for Parkinson's disease and other neurodegenerative disorders. By investigating the function of SNCAIP, researchers can gain valuable insights into the disease pathology and potentially identify new treatment strategies aimed at modulating alpha-synuclein aggregation and neurotoxicity.
Immunohistochemistry of paraffin-embedded human kidney tissue using PACO52918 at dilution of 1:100.
Immunofluorescent analysis of Hela cells using PACO52918 at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Immunohistochemistry of paraffin-embedded human brain tissue using PACO52918 at dilution of 1:100.
Background:
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.
SNCAIP: 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. Defects in SNCAIP may be a cause of Parkinson disease (PARK). A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease 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. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. 6 isoforms of the human protein are produced by alternative splicing.Protein type: VesicleChromosomal Location of Human Ortholog: 5q23.2Cellular Component: presynaptic membrane; synaptic vesicle; cell soma; cytoplasmMolecular Function: identical protein binding; protein binding; ubiquitin protein ligase bindingBiological Process: regulation of neurotransmitter secretion; dopamine metabolic processDisease: Parkinson Disease, Late-onset
UniProt Protein Details:
NCBI Summary:
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2015]
