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M2694

Sigma-Aldrich

Anti-Munc-18-1 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Munc-18α, Anti-STXBP1, Anti-Syntaxin-binding protein 1, Anti-rb-Sec-1

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About This Item

MDL number:
MFCD07370408
UNSPSC Code:
12352203
NACRES:
NA.41

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 67 kDa

species reactivity

mouse, rat

technique(s)

indirect immunofluorescence: 1:250-1:500 using mouse fibroblast NIH3T3 cell line
microarray: suitable
western blot: 1:2,000-1:4,000 using rat brain extract (S1 fraction) and PC12 whole cell extract.

UniProt accession no.

O08599

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... STXBP1(6812)
mouse ... Stxbp1(20910)
rat ... Stxbp1(25558)

General description

Munc-18-1 (67 kDa) is an abundant neuronal protein that tightly binds to the synaptic fusion protein syntaxin. It is primarily expressed in neuronal tissues. Both Munc-18-1 and 2 isoforms bind tightly to syntaxins 1A, 2, and 3.

Immunogen

synthetic peptide corresponding to amino acids 577-594 located at the C-terminus of rat Munc-18-1 conjugated to KLH. This sequence is identical in mouse, chicken, bovine, and human Munc-18-1. It does not share homology with the Munc-18-2 and Munc-18-3 isoforms.

Application

Anti-Munc-18-1 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

Munc-18-1 functions in synaptic vesicle exocytosis. It modulates neurotransmission by associating with syntaxin 1. Munc-18-1 binds to both syntaxin 1A and 1B isoforms, inhibiting the binding of t-soluble N-ethylmaleimide-sensitive factor-attached protein receptor (SNARE) synaptobrevin/vesicle-associated membrane protein (VAMP) and SNAP25 to syntaxin 1 and preventing SNARE assembly. Munc-18 is required for neurotransmitter secretion from synaptic vesicles throughout development and has been implicated in axonal branching in hippocampal neurons.

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 Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Gülçin Vardar et al.
eLife, 10 (2021-08-25)
Syntaxin-1 (STX1) and Munc18-1 are two requisite components of synaptic vesicular release machinery, so much so synaptic transmission cannot proceed in their absence. They form a tight complex through two major binding modes: through STX1's N-peptide and through STX1's closed
Mints as adaptors Direct binding to neurexins and recruitment of munc18
Biederer T and Sudhof TC
Test, 275(51), 39803-39806 (2000)
Ouada Nebie et al.
Brain : a journal of neurology, 144(10), 3142-3158 (2021-06-05)
Traumatic brain injury (TBI) leads to major brain anatomopathological damages underlined by neuroinflammation, oxidative stress and progressive neurodegeneration, ultimately leading to motor and cognitive deterioration. The multiple pathological events resulting from TBI can be addressed not by a single therapeutic
Ouada Nebie et al.
Journal of biomedical science, 26(1), 89-89 (2019-11-02)
Effective neurorestorative therapies of neurodegenerative diseases must be developed. There is increasing interest in using human platelet lysates, rich in neurotrophic factors, as novel disease-modifying strategy of neurodegeneration. To ensure virus safety, pathogen reduction treatments should be incorporated in the
Lucio M Schiapparelli et al.
Cell reports, 38(4), 110287-110287 (2022-01-27)
Intercellular transfer of toxic proteins between neurons is thought to contribute to neurodegenerative disease, but whether direct interneuronal protein transfer occurs in the healthy brain is not clear. To assess the prevalence and identity of transferred proteins and the cellular
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