Cat. No.: 106 104
Amount: 100 µl
Price:
$375.00
|
|
|
| Cat. No. 106 104 |
100 µl antiserum, lyophilized. For reconstitution add 100 µl H2O, then aliquot and store at -20°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
| Applications | |
| Immunogen | Synthetic peptide corresponding to AA 445 to 462 from mouse Synapsin1 (UniProt Id: O88935) |
| Reactivity |
Reacts with: mouse (O88935), rat (P09951). Other species not tested yet. |
| Specificity | Specific for synapsins 1a and 1b, no cross-reactivity to synapsin 2a/b. K.O. validated |
| Matching control protein/peptide | 106-1P |
| Remarks |
EM: This antibody has been successfully used and published for this application by customers (see “application” references). |
| Data sheet | 106_104.pdf |
|
|
Synapsins are neuron-specific phosphoproteins that play a fundamental role in synaptic vesicle trafficking and neurotransmitter release. They are exclusively associated with small synaptic vesicles in presynaptic terminals, with little or no expression in non-neuronal tissues including neuroendocrine cells (1–4). In mammals, three distinct genes—SYN1, SYN2, and SYN3—encode more than eight isoforms through alternative splicing. Synapsin1 is one of the most specific markers of synapses throughout both the central and peripheral nervous systems. In addition to presynaptic terminals, it is localized to sensory nerve endings and peripheral innervation of the gastrointestinal tract, including the small intestine, where it contributes to neurotransmitter release in enteric and extrinsic nerves (2,3). Two splice variants, synapsin1a and synapsin1b, interact with synaptic vesicle membranes and the cytoskeletal proteins actin and spectrin (1). Synapsin2, also expressed in the nervous system, exists in at least two splice variants, whereas synapsin3 displays a more restricted distribution, being enriched in hippocampal neurons and developing neural circuits (4).
Synapsins are major neuronal phosphoproteins and substrates of several kinases, including PKA, CaMK I, and CaMK II, with synapsin1 serving as a reference substrate for calmodulin-dependent protein kinases (1,4). Beyond their established neuronal role, recent studies have implicated synapsins in glioblastoma biology. In particular, synapsin3 has been shown to promote neuronal-like differentiation of glioblastoma stem cells by antagonizing Notch signaling, thereby reducing tumor stemness and progression (5). Moreover, glioblastoma cells can exploit synaptic communication pathways, underscoring a broader role for synaptic proteins in tumor growth and plasticity (6).