Phospho-SYN1 (S605) Antibody
Description
Definition and Target Specificity
Phospho-SYN1 (S605) Antibody detects the phosphorylated form of Synapsin-1 (SYN1), a neuronal phosphoprotein that modulates synaptic vesicle trafficking, neurotransmitter release, and synaptogenesis. The antibody specifically recognizes Ser605 phosphorylation, a site implicated in activity-dependent synaptic plasticity .
Monoclonal Antibody (CST #88246)
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Clonality: Rabbit monoclonal (Clone D4B9I)
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Applications: Western Blotting (1:1000 dilution)
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Sensitivity: Endogenous protein detection
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Storage: Supplied in liquid form; stability data not specified.
Polyclonal Antibody (STJ91309)
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Clonality: Rabbit polyclonal
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Applications: IHC (1:100–1:300), IF (1:200–1:1000), ELISA (1:20,000)
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Formulation: PBS with 50% glycerol, 0.5% BSA, 0.02% sodium azide
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Storage: Stable at -20°C for 1 year; avoid freeze-thaw cycles .
Phosphorylation-Regulated Synaptic Vesicle Dynamics
A 2022 study demonstrated that Ser605 phosphorylation inversely regulates Synapsin-1 palmitoylation, a lipid modification critical for its interaction with F-actin :
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Phosphorylation at Ser605 reduces Synapsin-1 palmitoylation, weakening its binding to F-actin and dispersing synaptic vesicles (SVs) .
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Depalmitoylation induced by phosphorylation enhances SV mobility, facilitating neurotransmitter release during synaptic activity .
Experimental Data Highlights
| Condition | Effect on Synapsin-1 | Impact on SVs |
|---|---|---|
| Forskolin-induced phosphorylation | ↓ Palmitoylation, ↓ F-actin binding | SV dispersion, reduced clustering |
| Ser605 dephosphorylation | ↑ Palmitoylation, ↑ F-actin binding | SV reclustering post-activity |
| Mutant Syn1-S605A (non-phosphorylatable) | No palmitoylation changes, sustained F-actin binding | Impaired SV mobilization during stimulation |
Biological Significance
Synapsin-1 phosphorylation at Ser605 is part of a regulatory crosstalk with palmitoylation, modulating synaptic vesicle pools:
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Activity-Dependent Plasticity: Phosphorylation during synaptic activity promotes SV mobilization, while dephosphorylation stabilizes SV clusters .
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Disease Relevance: Dysregulation of Synapsin-1 phosphorylation is linked to neurological disorders, though direct associations with Ser605 remain under investigation .
Usage Guidelines
Product Specs
Target Background
- Researchers identified the c.236 C > G/p.S79W mutation in SYN1 as the cause of non-syndromic intellectual disability in the MRX50 family. In vitro analysis of the S79W SynI mutation revealed that it does not interfere with neurodevelopmental aspects but disrupts spontaneous synaptic vesicle exocytosis, vesicle clustering, and lateral mobility along axons. PMID: 28973667
- These findings support previous research demonstrating dysregulation of Synapsins, particularly SYN2, in mood disorders. They enhance our understanding of the regulatory mechanisms that contribute to these changes, potentially leading to the development of bipolar disorder or major depressive disorder phenotypes. PMID: 27515700
- Cerebral malaria causes presynaptic excitation and ultimately activation of synapsin I, leading to increased neurotransmitter release. PMID: 26823711
- The patterns of immunoreactivity with antibodies to SNAP-25, synapsin-I and synaptophysin are fully consistent with those observed in the olfactory bulb of adults at 38-40 weeks of prenatal development. PMID: 26204769
- The implementation of the AlphaScreen pSYN1 assay and the future development of additional primary neuronal high-throughput screening assays provide a promising approach for the discovery of novel classes of therapeutic candidates for a variety of central nervous system disorders. PMID: 24088370
- These findings suggest that PRICKLE1 mutations contribute to autism spectrum disorder by disrupting the interaction with SYN1 and the regulation of synaptic vesicles. PMID: 24312498
- Data indicate that in patients carrying the W356x mutation, the function of synapsin I is significantly impaired. This supports the value of Syn1(-/-) mice as an experimental model mimicking the human pathology. PMID: 23818987
- The epileptogenic Q555X SYN1 mutant triggers imbalances in release dynamics and short-term plasticity. PMID: 23406870
- Histone modification marks were significantly increased in major depression and this effect was correlated with significant increases in SYN1b gene expression. PMID: 22571925
- The allelic frequencies of SYN1 are associated with Korean female schizophrenia. PMID: 22807112
- SYN1 loss-of-function mutations in autism and partial epilepsy cause impaired synaptic function. PMID: 21441247
- The nucleocytoplasmic shuttling of dysbindin-1 regulates synapsin I expression and may therefore be involved in the pathogenesis of schizophrenia. PMID: 20921223
- The authors propose that claudin-2 and SYN1 work together to enhance microbial translocation across the intestinal epithelial barrier, contributing to chronic immune activation and CD4 T-cell depletion in HIV-1-infected patients. PMID: 20700059
- The results showed that synapsin I was significantly decreased in the stratum radiatum of the CA1 subfield and the molecular layer of the dentate gyrus in Alzheimer's disease patients. PMID: 14673601
- A SYN1 nonsense mutation is the likely cause of epileptic and other phenotypes. PMID: 14985377
- Synapsins and S100A1 interact in nerve terminals where they are co-expressed. S100A1 cannot bind to synaptic vesicle-associated synapsin I and may function as a cytoplasmic store of monomeric synapsin I. Synapsin dimerization and interaction with S100A1 are mutually exclusive. PMID: 15147519
- This study concluded that the human synapsin I gene is positively regulated by nuclear respiratory factor 1 and mediates the function of nuclear respiratory factor 1 in neurite outgrowth. PMID: 19301426
