Recombinant Rat Synaptotagmin-1 (SYT1) Protein (His)

Name: Recombinant Rat Synaptotagmin-1 (SYT1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02024P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Synaptotagmin-1 (SYT1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P21707
Target Symbol	SYT1
Synonyms	(Synaptotagmin I)(SytI)(p65)
Species	Rattus norvegicus (Rat)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MVSASHPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK
Expression Range	1-421aa
Protein Length	Full Length
Mol. Weight	53.5 kDa
Research Area	Cancer
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	Calcium sensor that participates in triggering neurotransmitter release at the synapse. May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes.; (Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides. BoNT/B toxin binds to the membrane proximal vesicular domain of Syt1 (residues 32-51).; (Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); unlike the case with BoNT/B, interaction is not improved in the presence of gangliosides. BoNT/G toxin binds to the vesicular domain of Syt1 (residues 32-53).
Subcellular Location	Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm.
Protein Families	Synaptotagmin family
Database References	KEGG: rno:25716 STRING: 10116.ENSRNOP00000049624 UniGene: PMID: 29115943 Study showed postsynaptic localization of synaptotagmin 1, at concentrations moderately lower than, but comparable to presynaptic concentrations. It is present in significant concentrations at the postsynaptic density, pointing to the likelihood of insertion of glutamate receptors directly into the synaptic plasma membrane. Synaptotagmin 1 is reduced in postsynaptic spines after eight weeks of kainite-induced epilepsy. PMID: 28686803 The authors show that synaptotagmin-1 (from Rattus norvegicus and expressed in Escherichia coli) binds to phosphatidylinositol 4,5-diphosphate via a polybasic lysine patch in the C2B domain, which may promote the priming or docking of synaptic vesicles. PMID: 27791979 In this study, the authors show that the C2B domain of Syt1 interacts simultaneously with acidic membranes and SNARE complexes via the top Ca(2+)-binding loops, the side polybasic patch, and the bottom face in response to Ca(2+). PMID: 27083046 Data suggest that GTP-binding protein beta/gamma (Gb/g) heterodimers interact specifically with lipid-embedded neuronal t-SNARE proteins syntaxin 1A and SNAP-25B (synaptosomal-associated protein 25B); this binding is competitive with synaptotagmin 1 for binding sites on the t-SNARE proteins; Gb/g inhibits Ca2+/synaptotagmin 1-dependent membrane fusion. PMID: 28515322 After single synaptic vesicle fusion, syt1 acted as an essential determinant of synaptic vesicle endocytosis time course by delaying the kinetics of vesicle retrieval in response to increasing Ca(2+) levels. PMID: 28111077 Substitution of 4 Syt1 residues, YHRD, at C2 domain interface, disrupted interaction between tandem C2 domains, altered intrinsic affinity of Syt1 for Ca(2+), and shifted Ca(2+) dependency for binding to membranes and driving membrane fusion. YHRD mutant yielded reductions in synaptic transmission in neurons. Thus physical interactions between tandem C2 domains of syt1 contribute to excitation-secretion coupling. PMID: 26792839 Study indicates that the accumulation of Synaptotagmin1 may play an important role in axon/dendrite differentiation PMID: 26667128 different structural states of syt underlie the control of distinct forms of synaptic transmission. PMID: 27001899 The interaction of Dvl1 with Syt-1, which is regulated by Wnts, modulates neurotransmitter release. PMID: 26400647 Syt-1 regulates endogenous APP-CTF and Abeta levels in PC12 cells. Syt-1 knockdown reduces APP-CTF, sAPPbeta and Abeta levels. Secreted sAPPbeta levels were significantly reduced in PC12 cells lacking Syt-1 expression. PMID: 26202512 Membrane interaction of synaptotagmin-1 rather than SNARE binding triggers exocytosis of vesicles. PMID: 26389740 NMR approach reveals a dynamic binding mode in which basic residues in the concave side of the Syt1 C2B-domain beta-sandwich interact with a polyacidic region of the SNARE complex formed by syntaxin-1 and SNAP-25. PMID: 26030874 Modifications in the 60-residue linker modulate both the oligomerization of Syt1 and its interaction with opposing bilayers. In addition, the oligomerization of Syt1 may play a role in organizing proteins within the active zone of membrane fusion. PMID: 24973220 Data suggest that due to the intrinsic copper binding properties of the protein, a pre-labelling approach is preferred for the C2Ac domain of synaptotagmin I when copper is the desired radioisotope. PMID: 23954480 Analysis of SNARE complex/synaptotagmin-1 interactions by one-dimensional NMR Spectroscopy PMID: 23617808 the flexible linker region of Syt1 undergoes conformational changes during vesicle fusion: it stretches out to mediate vesicle docking, but folds to assist the C2AB domain for fusion pore opening. PMID: 24001110 Down-regulation of synaptotagmin 1 in cortex, hippocampus, and cerebellum is associated with experimental subarachnoid hemorrhage. PMID: 23884218 Iodine deficiency and propylthiouracil treatment reduce synaptotagmin-1 and PSD-95 in the rat hippocampus. PMID: 23321072 Using PC12 cells from Rattus norvegicus and artificial supported bilayers, authors show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca(2+) through phosphatidylinositol 4,5-bisphosphate. PMID: 23665582 This study demonistrated that synaptotagmin 11 distribution in neuron of rat hippocampus and presynapse and postsynapse. PMID: 22960622 Synaptotagmin I regulates patterned spontaneous activity in the developing rat retina via calcium binding to the C2AB domains. PMID: 23091625 It appears that SNAREs alone are sufficient in promoting membrane hemifusion, although Syt1 and Ca2+ are required to carry over toward pore formation and expansion. PMID: 23300284 synaptotagmin isoforms localize to distinct secretory organelles in both axons and dendrites and may regulate neuropeptide/neurotrophin release to modulate neuronal function. PMID: 22398727 vesicles have a threshold for syt I that is required to control opening of the fusion pore, expansion, and full fusion to release large dense core proteins, but not for full fusion of small molecules PMID: 22609930 Trans-interactions of synaptotagmin considered to be essential for its function are controlled by a delicate balance between cis- and trans-binding, which may play an important modulatory role in synaptic transmission. PMID: 22711810 Dysregulation of SNARE complex and syt-1 in prefrontal cortex of adult-onset hypothyroidism can be restored by T(4) treatment. PMID: 21646859 PIP(2) makes synaptotagmin-1 >40-fold more sensitive to Ca(2+). This interplay between Ca(2+), synaptotagmin-1, and PIP(2) is crucial for neurotransmitter release. PMID: 22447935 for Syt1 to function as a Ca2+ sensor, a charge asymmetry appears to be important and this may play a role in steering Syt1 to productively trans bind to the plasma membrane PMID: 22229667 Synaptotagmin I binds to syntaxin 1 electrostatically through C(2)B domain effector region in a Ca(2+)-independent fashion, providing biochemical evidence that synaptotagmin I binds SNARE complexes before Ca(2+) influx into presynaptic nerve terminals. PMID: 22008253 syt1 might facilitate SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors)-mediated membrane fusion by phase separating PS PMID: 21610074 These results suggest a conserved lipid binding mechanism in which Ca(2+)-independent interactions are mediated via a lysine rich region of the C2B domain while Ca(2+)-dependent interactions are mediated via the Ca(2+)-binding loops. PMID: 21928778 Data suggest that immature medial nucleus of the trapezoid body terminals may contain two populations of synaptic vesicles, one expressing VGLUT3 with synaptotagmin 2 and another expressing VGLUT3 with synaptotagmin 1. PMID: 21456023 Immunocytochemistry in rat chromaffin cells indicated that Syt1 was localized in large dense-core vesicles and synaptic-like microvesicles, whereas Syt7 was the predominant isoform present in large dense-core vesicles. PMID: 21287204 investigation of interaction of synaptotagmin 1 (and it's domains) with membrane bilayer PMID: 21344950 lipid-binding properties of 2 domains of Syt1: C2A domain selectively binds to disordered domains; C2B domain selectively binds to ordered domains PMID: 21322640 This analysis showed that C2AB domain of synaptotagmin and Ca(2+) accelerate vesicle-vesicle docking with more than two orders of magnitude. PMID: 21320440 The Syt7 C2B domain structure is very similar to that of the Syt1 C2B domain and contains three Ca2+-binding sites. PMID: 20824061 Data show that Syt I produced more rapid dilation of fusion pores than syt VII or syt IX, consistent with its role in synchronous synaptic release. PMID: 20573977 The results suggest that when associated with the SNAREs, syt1 is configured to bind opposing bilayers, but that the syt1/SNARE complex samples multiple conformational states. PMID: 21087613 the interplay between tomosyn and synaptotagmin-1 underlies inhibitory control of Ca(2+)-dependent neurotransmitter release. PMID: 20978127 These data support an inhibitory effect of syt IV on release of vesicles and their transmitter content which became more pronounced when syt I expression was abolished PMID: 20735850 findings show Syt1 requires the membrane anchor to stimulate vesicle fusion at physiological Ca2+ levels and may function as a dynamic presynaptic Ca2+ sensor to control the probability of neurotransmitter release PMID: 20448186 isolated an SYT1-associated endocytic complex (SAE) from presynaptic nerve terminals and used a novel fractional recovery assay based on electrostatic dissociation to identify SAE components and map the complex structure. PMID: 17183698 phosphorylation-dependent interaction with cysteine string protein PMID: 11931641 The InsP6 binding notably weakened the Ca(2+)-dependent C2AB-membrane interaction, which suggests that InsP6 may act as a modulator of neurotransmitter release by altering the state of synaptotagmin-phospholipid interaction. PMID: 12220627 structure and binding to a truncated neuronal SNARE complex PMID: 12496247 calcium-independent properties of Syt 1 regulate voltage-gated Ca2+ channels and contribute to the molecular events underlying transmitter release PMID: 12645522 analysis of palmitoylation sites and processing of synaptotagmin I PMID: 12782290 The synaptotagmin C2A domain is part of the calcium sensor controlling fast synaptic transmission. PMID: 12873386

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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.

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Recombinant Rat Synaptotagmin-1 (SYT1) Protein (His)

Recombinant Rat Synaptotagmin-1 (SYT1) Protein (His)

Product Overview

Target Details

FAQs