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Validated All-in-One™ qPCR Primer for SNCAIP(NM_005460.3) Search again
Product ID:
HQP023002
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
SYPH1, Sph1
Gene Description:
synuclein alpha interacting protein
Target Gene Accession:
NM_005460.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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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. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but their full-length nature has yet to be determined. [provided by RefSeq].
Gene References into function
- 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.
- results suggest that 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
- a causative role of the R621C mutation in the synphilin-1 gene in Parkinson's disease
- Changes in synuclein expression presage neurodegeneration in a Drosophila model of Parkinson disease.
- Siah-1 was found to abrogate the inhibitory effects of synphilin-1 on dopamine release
- role of aggresomes in cell viability was addressed in the context of over-expressing alpha-synuclein and its interacting partner synphilin-1
- Casein kinase II (CKII) phosphorylates synphilin-1; beta subunit of this enzyme complex binds to synphilin-1. CKII-mediated phosphorylation of synphilin-1, rather than alpha-synuclein, modulates the aggregation into inclusion bodies.
- role of synphilin-1 in synaptic function and protein degradation and in the molecular mechanisms leading to neurodegeneration in Parkinson disease
- Parkin is a dual-function ubiquitin ligase. K63-linked ubiquitination of synphilin-1 by parkin may be involved in the formation of Lewy body inclusions associated with Parkinson disease.
- We confirm that synphilin-1 and parkin are components of majority of Lewy Bodies in Parkinson's disease and that both proteins are susceptible to proteasomal degradation.
- GSK3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH
- Synphilin-1A may contribute to neuronal degeneration in alpha-synuclein mutations and provides insights into the role of inclusion bodies in neurodegenerative disorders.
- These results suggest that NUB1 indeed targets synphilin-1 to the proteasome for its efficient degradation, which, because of the resultant reduction in synphilin-1, suppresses the formation of synphilin-1-positive inclusions.
- a novel specific interaction of synphilin-1 with the regulatory proteasomal protein S6 ATPase (tbp7) in aggresome-like intracytoplasmic inclusions
- These findings suggest that parkin and synphilin-1 isoform expression changes play a significant role in the pathogenesis of LB diseases.
- review:Isoform Synphilin-1A inclusions recruit both alpha-synuclein and synphilin-1. Aggregation of synphilin-1 and synphilin-1A seems to be protective to cells
- specific effects of C621 mutant synphilin-1 on gene expression that correlate with its role as a susceptibility factor in Parkinson's disease
- We found no evidence for association between genetic variability in synphilin-1 and Parkinson's disease
- translocation to aggresomes required a special aggresome-targeting signal within the sequence of synphilin 1, an ankyrin-like repeat domain.