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Synaptotagmin I (SYT1) (AA 10-60) antibody

Details for Product No. ABIN350924, Supplier: Log in to see
Antigen
  • CG3139
  • D. Syt I
  • DSYT
  • DSYT2
  • DSypt
  • DSyt
  • Dmel\\CG3139
  • Droso1
  • Dsyt2
  • SYT
  • SYT I
  • SYT1
  • Syt
  • Syt 1
  • Syt I
  • Syt-1
  • SytI
  • dSYT
  • dsyt1
  • dsytI
  • l(2)23AB1
  • l(2)23Ba
  • l(2)k05909
  • syt
  • syt 1
  • syt I
  • syt-1
  • syt1
  • sytI
  • Syti
  • GB20036
  • svp65
  • DKFZP459P193
  • 5430411C10Rik
  • GOLPH5
  • GRASP65
  • P65
  • SVP65
  • AW124717
  • G630098F17Rik
  • p65
Epitope
AA 10-60
28
19
16
15
12
10
5
3
3
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Mouse (Murine)
169
88
85
9
8
6
5
3
3
2
1
1
1
1
1
1
Host
Rabbit
144
29
16
6
5
2
Clonality
Polyclonal
Conjugate
Un-conjugated
9
9
9
3
3
3
2
2
2
2
2
2
2
2
2
Application
Immunohistochemistry (IHC), Western Blotting (WB)
159
73
71
26
24
22
14
10
3
2
2
2
1
Supplier
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Immunogen A synthetic peptide from aa region 10-60 of rat Synaptotagmin 1 conjugated to blue carrier protein was used as the antigen. The antigen is homologous in mouse.
Isotype IgG
Specificity Specific for SYTI.
Alternative Name Synaptotagmin 1 (SYT1 Antibody Abstract)
Background Function: 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.
Cofactor: Binds 3 calcium ions per subunit. The ions are bound to the C2 domains.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Note: Synaptic vesicles and chromaffin granules.
Tissue specificity: Predominantly expressed in rostral, phylogenetically younger brain regions, and in some endocrine tissues. Also known as: Synaptotagmin-1, Synaptotagmin I, SytI, p65, SVP65.
Research Area Neurology
Pathways
Application Notes A concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 500 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Schivell, Mochida, Kensel-Hammes et al.: "SV2A and SV2C contain a unique synaptotagmin-binding site." in: Molecular and cellular neurosciences, Vol. 29, Issue 1, pp. 56-64, 2005 (PubMed).

Heindel, Schmidt, Veit: "Palmitoylation sites and processing of synaptotagmin I, the putative calcium sensor for neurosecretion." in: FEBS letters, Vol. 544, Issue 1-3, pp. 57-62, 2003 (PubMed).

Fernandez, Arauc, Ubach et al.: "Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine." in: Neuron, Vol. 32, Issue 6, pp. 1057-69, 2001 (PubMed).

Coppola, Magnin-Luthi, Perret-Menoud et al.: "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin." in: The Journal of biological chemistry, Vol. 276, Issue 35, pp. 32756-62, 2001 (PubMed).

Shao, Fernandez, Suedhof et al.: "Solution structures of the Ca2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change?" in: Biochemistry, Vol. 37, Issue 46, pp. 16106-15, 1998 (PubMed).

Schivell, Batchelor, Bajjalieh: "Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin." in: The Journal of biological chemistry, Vol. 271, Issue 44, pp. 27770-5, 1996 (PubMed).

Sutton, Davletov, Berghuis et al.: "Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold." in: Cell, Vol. 80, Issue 6, pp. 929-38, 1995 (PubMed).