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

Beta LifeScience SKU/CAT #: BLC-04426P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

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

Beta LifeScience SKU/CAT #: BLC-04426P
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Product Overview

Description Recombinant Human Synaptotagmin-1 (SYT1) Protein (His) is produced by our E.coli expression system. This is a cytoplasmic protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P21579
Target Symbol SYT1
Synonyms DKFZp781D2042; FLJ42519; p65; SVP65; Synaptotagmin 2; Synaptotagmin I; Synaptotagmin II; Synaptotagmin-1; SYT; Syt1; SYT1_HUMAN; Syt2; SytI
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence KNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDA
Expression Range 99-416aa
Protein Length Cytoplasmic Domain
Mol. Weight 40.3kDa
Research Area Neuroscience
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.
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

HGNC: 11509

OMIM: 185605

KEGG: hsa:6857

STRING: 9606.ENSP00000261205

UniGene: PMID: 28130000

  • The MD simulations revealed that all peptides induced significant Syt1 rigidity by binding in the cleft of the C2A-C2B interface. The consequence of this binding event is the suppression of the protein motion associated with conformational change of Syt1 from the closed form to the open form. PMID: 29019108
  • Although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3. PMID: 28696301
  • Circular oligomerization is an intrinsic property of SYT1. PMID: 28850328
  • that reduction in the synaptotagmin 1 level and presenilin 1-synaptotagmin 1 interactions in AD brain may present molecular underpinning of the pathogenic presenilin 1 conformation PMID: 28193235
  • findings show extended Synaptotagmi1 (E-Syt1), along with related E-Syt3, negatively modulates viral release into the extracellular milieu, cell-to-cell viral spread and viral entry, processes that implicate membrane fusion events; , these E-Syt proteins impacted formation of virus-induced syncytia; findings hint at the modulation of the viral fusion machinery by the E-Syt family of proteins PMID: 29046455
  • Using electron microscopy combined with targeted mutations, the authors show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca(2+) involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission. PMID: 27434670
  • This study found that the CSF levels of synaptotagmin-1 were consistently elevated in patients with dementia due to Alzheimer's disease. PMID: 27716408
  • SYT-SSX fusion is associated with synovial sarcoma. PMID: 27621063
  • the extended synaptotagmins (E-Syts), endoplasmic reticulum (ER) proteins that function as PtdIns(4,5)P2- and Ca(2+)-regulated tethers to the Pplasma membrane. PMID: 27065097
  • Data indicate that small protein sequence changes in the Ca(2+)-binding loops of the C2 domains may give rise to the difference in binding kinetics between Syt-1 and Syt-7 isoforms. PMID: 27997124
  • These findings identify Syt1 as a novel Ca(2+)-sensitive PS1 modulator that could regulate synaptic ABETA, opening avenues for novel and selective synapse targeting therapeutic strategies. PMID: 27036734
  • One-Step reverse transcriptase real time PCR for the detection SYT-SSX transcript is feasible as an aid in confirming the diagnosis of synovial sarcoma. PMID: 27126659
  • membrane tethering by E-Syt1 (ER to PM) and by synaptotagmin (secretory vesicles to PM) undergo a similar regulation by plasma membrane lipids and cytosolic Ca(2+). PMID: 26202220
  • A dominant negative de novo SYT1 missense variant(I368T)altered the kinetics of synaptic vesicle endocytosis and caused an early onset dyskinetic movement disorder, severe motor delay, and profound cognitive impairment. PMID: 25705886
  • Data suggest that calcium-dependent phosphatidylinositol 4,5-diphosphate- (PI(4,5)P2-) binding proteins (such as SYT1, PRKCA [protein kinase C alpha], and ANXA2 [annexin A2]) interactions with membrane microdomains are tightly regulated. [REVIEW] PMID: 25233429
  • Whole genome analyses of a well-differentiated liposarcoma reveals novel SYT1 and DDR2 rearrangements. PMID: 24505276
  • Hydrophobic interactions play a key role in Syt1 binding botulinum neurotoxin DC. PMID: 23932591
  • Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1. PMID: 24302762
  • synaptotagmin-1 is involved in a rapid vesicular Ca(2) sequestration through a Ca(2)/H antiport PMID: 23607712
  • PRIP inhibits regulated exocytosis through the interaction of its C2 domain with syntaxin 1 and SNAP-25, potentially competing with accessory proteins such as synaptotagmin I and by directly inhibiting trans-SNARE complex formation PMID: 23341457
  • Characterization of negative coupling interaction between the C2 domains of Syt I. PMID: 23071627
  • The mechanistic basis for C2A domain of synaptotagmin I's response to Ca(2+) and cellular function stems from marginal stability and ligand-induced redistributions of protein conformers. PMID: 22853901
  • The membrane dissociation of SYT7 C2A domain but not SYT1 C2A domain is slowed by Na(2)SO(4) and trehalose, solutes that enhance the hydrophobic effect. PMID: 22966849
  • Together with synaptotagmin 1, complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca(2+) concentrations. PMID: 22705946
  • The calcium binding site to the C2A domain of SYT1 has been identified; this SYT1 domain activates exocytosis of secretory vesicles during neurotransmitter release. PMID: 22475172
  • association between serum creatinine level and polymorphisms in the collagen type XXII alpha 1 (COL22A1) gene, on chromosome 8, and in the synaptotagmin-1 (SYT1) gene, on chromosome 12 PMID: 20222955
  • NMR characterization of copper and lipid interactions of the C2B domain of synaptotagmin I-relevance to the non-classical secretion of the human acidic fibroblast growth factor (hFGF-1). PMID: 19835837
  • intestinal epithelial Syt 1 plays an important role in cAMP-stimulated endocytosis of apical NHE3 through cAMP-dependent phosphorylation of S605 that is required for NHE3 and Syt 1 association PMID: 19926819
  • synaptotagmin-I expressing neuroblastoma cells require gangliosides for Botulinum neurotoxin A activity PMID: 12089155
  • both synaptotagmins I and II can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25) dimer PMID: 14709554
  • Syt I mediates cAMP- and Ca(2+)-induced endocytosis of NHE3 through cargo recognition of NHE3 and subsequent recruitment of AP2-clathrin assembly required for membrane endocytosis. PMID: 17307723
  • The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. PMID: 17956130
  • These findings provide new information in the epileptogenesis of refractory epilepsy, and suggest that Synaptotagmin I might be involved in human refractory epilepsy. PMID: 18779938
  • mechanical stability of the C2A and C2B domains of human Syt1 PMID: 19186144

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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.

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