Recombinant Rat Synapsin-1 (SYN1) Protein (His)

Name: Recombinant Rat Synapsin-1 (SYN1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06527P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Rat Synapsin-1 (SYN1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P09951
Target Symbol	SYN1
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	ARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQALPR
Expression Range	113-420aa
Protein Length	Partial
Mol. Weight	35.6 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.
Subcellular Location	Cell junction, synapse. Golgi apparatus.
Protein Families	Synapsin family
Database References	KEGG: rno:24949 STRING: 10116.ENSRNOP00000014250 UniGene: Rn.9923

Gene Functions References

The synapsin 1 in the insular cortex as a part of pathophysiological process that determines predisposition of Krushinsky-Molodkina rats to audiogenic seizures. PMID: 26923581
SUMOylation of synapsin Ia (SynIa) at K687 is necessary for SynIa function. Replacement of endogenous SynIa with a non-SUMOylatable mutant decreases the size of the releasable vesicle pool and impairs stimulated SV exocytosis. PMID: 26173895
Results suggest a mechanism of A2aR modulation of neurotransmitter release in cultured cells from medulla oblongata and suggest that protein kinase A mediates this modulation of neurotransmitter release via synapsin I phosphorylation PMID: 24912137
rSynI(1.0)-minCMV drives robust and neuron-specific transgene expression throughout the CNS and is therefore useful for viral vector-mediated neuron-specific gene delivery and generation of neuron-specific transgenic animals. PMID: 24361760
This study demonistrated that Increased activation of synapsin 1 in the amygdala of maternal separation rats. PMID: 24279756
O-GlcNAcylation of Thr-87 interferes with folding of the ALPS motif, providing a means for regulating the association of synapsin I with SVs as a mechanism contributing to synapsin I localization and RPSV generation. PMID: 24280219
The mean brightness of Syn1 per unit area of the dendritic tree of neurons changes over the estrous cycle, being approximately 35% lower at diestrus than at the remaining phases of the estrous cycle. PMID: 21948316
A hybrid peptide consisting of synapsin carboxyl domain fused with E coli enterotoxin B subunit up-regulates expression of anti-inflammatory cytokines and diminishes myelin basic protein-specific T-helper cell responses in lymph nodes. PMID: 22138356
Syn I phosphorylation at site 1 regulates synapse formation. PMID: 22045728
Data provide a complete molecular pathway (GR/Egr-1/MAPK/Syn-Ia/Ib) through which stress and glucocorticoids enhance the memory of stress-related events and highlight the function of synapsin-Ia/Ib as molecular effector of the behavioral effects of stress PMID: 20368707
Data show that Src-mediated tyrosine phosphorylation of synapsin I increases its binding to synaptic vesicles and actin, and increases the formation of synapsin dimers, which are both potentially involved in vesicle clustering. PMID: 20530578
Data suggest that integrin-linked kinase exerts pleiotropic actions by regulating pre- and postsynaptic neural plasticities in response to repeated cocaine exposure through PSD-95 and synapsin I expression and GluR1 Ser845 phosphorylation. PMID: 19629758
Either C-terminal domain E or a peptide derived from domain C was necessary and sufficient to inhibit both dimerization and vesicle clustering, indicating the participation of both domains in these activities of synapsin I. PMID: 19922412
Seven days after fluid-percussion brain injury, synapsin I mRNA levels increase ipsilaterally and decrease contralaterally in the occipital cortex. PMID: 12184851
These results raise the possibility that Ser(603) on synapsin I is alternatively phosphorylated by p21-activated kinases, not only by CaMKII, in neuronal cells in response to some stimulants. PMID: 12237306
BEMAD methodology was validated by mapping three previously identified O-GlcNAc sites, as well as three novel sites, on Syn I. PMID: 12438562
multiple signaling pathways serve to allow synapsin's control of vesicle mobilization over different stimulus frequencies. PMID: 12691665
Time-dependent translocational changes of Synapsin I were investigated in regenerating axonal sprouts. PMID: 14612614
Calorimetric measurements of ATP binding to wild-type and mutant recombinant Synapsin I-ABC demonstrate that the multifunctional loop and a cross-tetramer contact are important for ATP binding PMID: 14688264
During the first postnatal week,synpsin 1 immunoreactive strongly concentrated in the Purkinje cell layer.By P14, synapsin 1 localized to many small puncta in the ML and to large clusters at mossy fiber rosettes in the glomerular layer. PMID: 15246689
glucose-dependent actions of ERK1/2 in beta-cells exerted on cytoplasmic proteins, includes synapsin I and participates in the overall glucose-induced insulin secretion. PMID: 15498890
In conclusion, this is the first evidence to show that PLD1 acts as an important regulator of neurite outgrowth in neural stem cell by promoting neuronal differentiation via increase of synapsin I expression. PMID: 15752728
findings show that synapsin I plays a central role in regulating the organization and dynamics of synaptic vesicles in growth cones and that this activity is modulated by cAMP-dependent phosphorylation of the protein PMID: 16093379
Neither haloperidol nor the dopamine-D1 receptor antagonist affected synapsin I protein expression. PMID: 16413126
These results suggest, therefore, that Ca2+ entrance mediated by P2X7 receptor induces glutamate release and in parallel synapsin-I phosphorylation. PMID: 18242779
Synapsin1a modulation by piccolo regulates synaptic vesicle exocytosis PMID: 18519737
Data suggest that diabetes has a profound impact on synapsin I and other presynaptic protein expression in the retina, and may provide a mechanism for the well-established defects in vision and the electrophysiological response of the retina in diabetes. PMID: 18662330
Synapsin I is embedded in open chromatin in R28 retinal precursor cells. PMID: 18692536
Data show that long-term amygdala kindling increases synapsin I immunoreactivity bilaterally in most hippocampal subfields, but not in the caudate nucleus, sensorimotor cortices, or piriform cortex in rats. PMID: 18703092
pentachlorophenol exposure during development causes thyroid function vulnerability, testicular hypertrophy in adults, and aberrations of brain gene expression of syn1 PMID: 19082768
mW/cm(2) (SAR 14.1 W/kg) microwave radiation can result in the perturbation of the synaptic vesicles associated proteins: synapsin I, synaptophysin, VAMP-2, and syntaxin PMID: 19603498

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.