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Merck

S2177

Sigma-Aldrich

Anti-Synaptotagmin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 65 kDa

species reactivity

rat

technique(s)

microarray: suitable
western blot: 1:5,000 using extract of rat brain membrane fraction

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SYT1(6857)
mouse ... Syt1(20979)
rat ... Syt1(25716)

General description

Synaptotagmin (Syt, p65) is an abundant synaptic vesicle (SV) membrane protein. It is characterized by a short intravesicular N-terminal domain, a single transmembrane region and two copies of highly conserved internal repeats, known as the C2A and C2B domains, which are homologous to the C2 regulatory region of protein kinase C (PKC) in the cytoplasmic domain. At least eight different isoforms of synaptotagmin (SytI-VIII) are expressed in the brain, four of which (Syt IV, V, VII and VIII) are also expressed in non-neuronal tissues.

Specificity

The sequence is highly conserved among species (SytI) and is not found in other known synaptotagmin isoforms (SytII-VIII).

Immunogen

synthetic peptide corresponding to N-terminus of synaptotagmin I (SytI) of rat origin (amino acids 1-16 with C-terminally added lysine), conjugated to KLH.

Application

Anti-Synaptotagmin antibody produced in rabbit has been used:
  • for cell surface labelling of synaptotagmin I (SytI)
  • in immunofluorescence microscopy
  • in western blotting

Biochem/physiol Actions

Synaptotagmin binds Ca2+ phospholipids with high affinity and has a central role in Ca2+ regulated neurotransmitter release. Synaptotagmin functions as a Ca2+ sensor and is required for efficient exocytosis, particularly in the vesicle docking and/or fusion step with the plasma membrane. Ca2+ influx triggers synaptotagmin to interact with either syntaxin or SNAP-25 and the cytoplasmic domain of neurexin leading to fusion and exocytosis. Mutations or deletion of synaptotagmin result in severely impaired Ca2+ triggered neurotransmitter release. Synapses of SytI knockout mice lack the fast-component of Ca2+ dependent neurotransmitter release, but exhibit no changes in the slow, Ca2+ independent component of synaptic vesicle exocytosis.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Tumor protein D52 controls trafficking of an apical endolysosomal secretory pathway in pancreatic acinar cells
Messenger SW, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 305(6), G439-G452 (2013)
The products of the Drosophila stoned locus interact with synaptic vesicles via synaptotagmin
Phillips AM, et al.
The Journal of Neuroscience, 20(22), 8254-8261 (2000)
Expression, localization, and functional role for synaptotagmins in pancreatic acinar cells
Falkowski MA, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 301(2), G306-G316 (2011)
Michelle A Falkowski et al.
American journal of physiology. Gastrointestinal and liver physiology, 301(2), G306-G316 (2011-06-04)
Secretagogue-induced changes in intracellular Ca(2+) play a pivotal role in secretion in pancreatic acini yet the molecules that respond to Ca(2+) are uncertain. Zymogen granule (ZG) exocytosis is regulated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes. In nerve
Gui-Hai Chen et al.
Neurobiology of aging, 28(4), 611-618 (2006-05-09)
The age-related decline of learning and memory is a common phenomenon in humans and animals, even though the underlying mechanism is not yet known. In the present study, we propose that synaptotagmin 1 (Syt 1) might be a synaptic protein

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