Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human SYT1 Antikörper:
anti-Mouse (Murine) SYT1 Antikörper:
anti-Rat (Rattus) SYT1 Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Polyclonal SYT1 Primary Antibody für IHC, WB - ABIN3016235
Shen, Xing, Cui, Li, Zhang, Du, Zhang, Li: MicroRNA-30a attenuates mutant KRAS-driven colorectal tumorigenesis via direct suppression of ME1. in Cell death and differentiation 2018
Show all 9 Pubmed References
Human Polyclonal SYT1 Primary Antibody für IHC, WB - ABIN6670055
Wan, Jin, Zhu, Fang, Mao, He, Xia, Li, Li, Chen, Hu: MicroRNA-149-5p regulates blood-brain barrier permeability after transient middle cerebral artery occlusion in rats by targeting S1PR2 of pericytes. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2019
Show all 9 Pubmed References
Rat (Rattus) Polyclonal SYT1 Primary Antibody für IHC, WB - ABIN361497
Fernández-Chacón, Königstorfer, Gerber, García, Matos, Stevens, Brose, Rizo, Rosenmund, Südhof: Synaptotagmin I functions as a calcium regulator of release probability. in Nature 2001
Show all 6 Pubmed References
Rat (Rattus) Polyclonal SYT1 Primary Antibody für IHC, WB - ABIN152576
Hilfiker, Pieribone, Nordstedt, Greengard, Czernik: Regulation of synaptotagmin I phosphorylation by multiple protein kinases. in Journal of neurochemistry 1999
Show all 4 Pubmed References
Chicken Polyclonal SYT1 Primary Antibody für ICC, IF - ABIN550172
Wang, Lu, Bai, Chang, Martin, Chapman, Jackson: Different domains of synaptotagmin control the choice between kiss-and-run and full fusion. in Nature 2003
Show all 3 Pubmed References
Chicken Polyclonal SYT1 Primary Antibody für ICC, IF - ABIN550191
Poskanzer, Marek, Sweeney, Davis: Synaptotagmin I is necessary for compensatory synaptic vesicle endocytosis in vivo. in Nature 2003
Show all 3 Pubmed References
Human Monoclonal SYT1 Primary Antibody für ELISA, WB - ABIN969429
Xu, Gammon, Zeisel, Lee, Wetmur, Teitelbaum, Bradshaw, Neugut, Santella, Chen: Choline metabolism and risk of breast cancer in a population-based study. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008
Show all 2 Pubmed References
Cow (Bovine) Polyclonal SYT1 Primary Antibody für WB - ABIN550163
Littleton, Bellen: Synaptotagmin controls and modulates synaptic-vesicle fusion in a Ca(2+)-dependent manner. in Trends in neurosciences 1995
Show all 3 Pubmed References
Rat (Rattus) Polyclonal SYT1 Primary Antibody für ICC, WB - ABIN1742200
Shinoda, Ahmed, Ramachandran, Bharat, Brockelt, Altas, Dean: BDNF enhances spontaneous and activity-dependent neurotransmitter release at excitatory terminals but not at inhibitory terminals in hippocampal neurons. in Frontiers in synaptic neuroscience 2014
The present study replicates previously suggested association of the SYT1-rs2251214 SNP with ADHD in adults.
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.
Although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3.
Circular oligomerization is an intrinsic property of SYT1.
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
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
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.
This study found that the CSF levels of synaptotagmin-1 were consistently elevated in patients with dementia due to Alzheimer's disease.
SYT-SSX fusion is associated with synovial sarcoma.
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.
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.
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.
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.
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+).
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.
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]
Whole genome analyses of a well-differentiated liposarcoma reveals novel SYT1 and DDR2 rearrangements.
Hydrophobic interactions play a key role in Syt1 binding botulinum neurotoxin DC.
Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1.
synaptotagmin-1 is involved in a rapid vesicular Ca(2) sequestration through a Ca(2)/H antiport
This study uncovered essential residues within Synaptotagmin that suggest a structural basis for several activities required for fusion, including a C2B domain surface implicated in SNARE complex interaction that is required for rapid synchronization and Ca(2+) cooperativity of vesicle release.
tethering of Syt1 to synaptic vesicles in vivo is a prerequisite for its role in facilitating fast synchronous synaptic vesicle release and suppressing asynchronous and spontaneous fusion
synaptic transmission can be regulated by Syt1 multimerization and that both C2 domains of Syt1 are uniquely required for modulating Ca(2+)-independent spontaneous fusion and Ca(2+)-dependent synchronous release.
effect of APP gene on synaptotagmin 1 mRNA level
The major function of Ca2+ binding to synaptotagmin's C2A domain is to neutralize the negative charge of the pocket, thereby unleashing the fusion-stimulating activity of synaptotagmin.
this study provided direct support for the hypothesis that plasma membrane penetration, specifically by the C(2)B domain of synaptotagmin, is the critical effector interaction for coupling Ca(2+) binding with vesicle fusion
Results suggest that the tandem C2 domains of Syt 1 play independent roles in neurotransmission.
The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo
Synaptotagmins I and IV promote transmitter release independently of Ca(2+) binding in the C(2)A domain
Data show that synaptotagmin I is required for a post-docking step during vesicle fusion but does not function to stabilize the docked vesicle state.
These results indicate that synaptotagmin is the major Ca(2+) sensor for evoked release and functions to trigger synchronous fusion in response to Ca(2+), while suppressing asynchronous release.
Syt I is necessary for the endocytosis of synaptic vesicles that have undergone exocytosis using a functional Syt I protein
synaptotagmin 1 is a negative regulator of vesicle fusion of synaptic transmission.
Elimination of synaptic transmission and decrease in Ca(2+) affinity of release observed in Ca(2+)-binding motif mutants is not due to altered synaptic vesicle distribution but rather is because of disrupting synaptotagmin I's ability to bind Ca(2+).
These results demonstrate that the polylysine motif is required for efficient Ca2+-independent docking and/or priming of synaptic vesicles in vivo.
Sr(2+) partially substitutes for Ca(2+) in synchronous release but does not support the negative regulatory function of Syt I.
Presence of two presynaptic calcium sensors in a biological context, one a calcium-based sensor devoted primarily to baseline synaptic transmission and a second sensor for short-term synaptic plasticity.
human APP gene plays role in synaptogenesis in transgenic lines of Drosophila melanogaster whose nerve cells express the human APP695 isoform, truncated APPs, and the presynaptic marker synaptotagmin driving the sequence of the green fluorescent protein.
Results demonstrate that synaptotagmin I plays a direct role in regulating spontaneous transmitter release, indicative of an active role in synaptic vesicle stabilization mediated by the C(2)A polylysine motif.
Mutating Ca(2+)-coordinating aspartates in the C2A-domain localizes Doc2B permanently at the plasma membrane, and renders an upstream priming step Ca(2+)-independent, whereas a separate function in downstream priming depends on SNARE-binding, Ca(2+)-binding to the C2B-domain of Doc2B, interaction with ubMunc13-2 and the presence of synaptotagmin-1.
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.
Authors propose that the strong reduction of Syt2 and SV2B are key factors of the functional synaptic alteration and that the physiological downregulation of Syt1 plays a determinant role in muscle vulnerability in SMA.
The function of synaptotagmin-1 (syt-1):soluble NSF attachment protein receptor (SNARE) interactions during neurotransmission remains unclear.
we identify Syt2 as a functionally important Ca(2+) sensor at fast-releasing inhibitory synapses, and show that Syt1 and Syt2 can redundantly control transmitter release at specific brain synapses
results suggest that postsynaptic Syt1 and Syt7 act as redundant Ca(2+)-sensors for Ca(2+)-dependent exocytosis of AMPA receptors during long-term potentiation, and thereby delineate a simple mechanism for the recruitment of AMPA receptors that mediates LTP
demonstrates a developmental Syt1-Syt2 isoform switch at an identified synapse, a mechanism that could fine-tune the speed, reliability, and plasticity of transmitter release at fast releasing CNS synapses.
the combined inactivation of all 3 E-Syt genes has no effect on mouse viability or fertility.
We conclude that synaptotagmin-1 phosphorylation is an essential step in PKC-dependent potentiation of synaptic transmission, acting downstream of the two other essential DAG/PKC substrates, Munc13-1 and Munc18-1.
data show that hepatic Syt1 expression is influenced by diet and hormonal milieu
different structural states of syt underlie the control of distinct forms of synaptic transmission.
The interaction of Dvl1 with Syt-1, which is regulated by Wnts, modulates neurotransmitter release.
Data (including data from studies in knockout mice) suggest that loss of both Syt1/Syt7 decreases capacity of readily-releasable pool (RRP) of Ca2+ in synaptic vesicles without altering rate of priming into RRP; Syt1/Syt7 functions appear redundant.
Syt-1 regulates Abeta levels in mouse neurons. Knockdown of endogenous Syt-1 in mouse primary neurons led to a significant reduction in both Abeta40 and Abeta42 generation.
Increased expression of Syt1 in neural stem cells is essential for neurogenesis progression.
This study provides new insights in how the two opposite sides of the C2B domain of Synaptotagmin-1 participate in secretory vesicle fusion, and in more upstream steps, especially vesicle docking.
atomic-resolution crystal structures of Ca(2+)- and Mg(2+)-bound complexes between synaptotagmin-1 and the neuronal SNARE complex
the Ca(2+) dependence of the interaction between PRIP-C2 and Syt1-C2A was attributed to Ca(2+) binding with Syt1-C2A, but not PRIP-C2, using a series of mutants prepared from both C2 domains.
Tissue-specific splicing, posttranslational modification and the variation in expression might suggest a different requirement of SYT1 for the specific function in each organ.
This protein binds to target SNAREs in synaptic vesicle exocytosis.
The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin-1 participates in triggering neurotransmitter release at the synapse (Fernandez-Chacon et al., 2001
, synaptoptagmin 1
, synaptotagmin I
, synaptotagmin p65
, DKFZP459P193 protein
, Synaptotagmin I
, synaptotagmin I VQ/C2B-beta
, synaptotagmin 1 L homeolog