The SNCAIP Antibody (PAC001566) offered by Assay Genie is a high-quality polyclonal antibody designed for research involving SNCAIP, a protein associated with Parkinson's disease. This antibody, raised in rabbits, is highly specific and reactive with human samples, making it a reliable tool for studying the role of SNCAIP in neurodegenerative disorders.SNCAIP, also known as alpha-synuclein interacting protein, is believed to play a crucial role in the regulation of alpha-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. Research into the function and interactions of SNCAIP may provide insights into the mechanisms underlying neurodegeneration, potentially leading to the development of novel therapeutic strategies for Parkinson's disease and related conditions.
The SNCAIP Antibody is validated for use in Western blot applications, enabling precise detection and analysis of SNCAIP expression in various cell types and tissues. Its specificity and sensitivity make it an invaluable tool for researchers studying the molecular mechanisms of neurodegenerative disorders and seeking to identify novel targets for therapeutic intervention.
Antibody Name:
SNCAIP Antibody
Antibody SKU:
PACO01566
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB, IHC
Recommended Dilutions:
WB:1:500-1:2000, IHC:1:100-1:300
Species Reactivity:
Human, Mouse
Immunogen:
synthesized peptide derived from the C-terminal region of human Synphilin-1.
Form:
Liquid
Storage Buffer:
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Synonyms:
SNCAIP; Synphilin-1; Sph1; Alpha-synuclein-interacting protein
UniProt Protein Function:
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]
