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S2194

Sigma-Aldrich

Anti-SNAP-23 (TS-19) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Synaptosomal-Associated Protein 23

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About This Item

MDL number:
UNSPSC Code:
12352203

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 23 kDa

species reactivity

mouse, rat

technique(s)

indirect immunofluorescence: 1:200 using mouse embryonic 3T3-LT cell line.
microarray: suitable
western blot: 1:1,000 using whole cell extract of mouse fibroblasts NIH3T3 cell

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SNAP23(8773)
mouse ... Snap23(20619)
rat ... Snap23(64630)

General description

Anti-SNAP-23 (TS-19) is developed in rabbit using a synthetic peptide corresponding to amino acids, located at the C-terminus, of mouse SNAP-23, conjugated to keyhole limpet hemocyanin (KLH) as immunogen. SNARE proteins are present on both vesicle membranes (vesicle SNAREs or vSNAREs) and on target membranes (target SNAREs or t-SNAREs). SNAP-23 (synaptosomal associated protein, 23 kDa, syndet), is a nonneuronal homolog of SNAP-25, originally identified in a human B-lymphocyte cDNA library in a yeast two-hybrid screen for proteins interacting with syntaxin. SNAP-23 is ubiquitously expressed.

Immunogen

synthetic peptide corresponding to amino acids 203-221 located at the C-terminus of mouse SNAP-23, conjugated to KLH. This sequence is identical in rat and highly conserved (84% identity) in human SNAP-23.

Application

Anti-SNAP-23 (TS-19) antibody produced in rabbit has been used in:
  • immunofluorescence
  • immunoblotting
  • immunoprecipitation

Biochem/physiol Actions

SNAP-23 (synaptosomal associated protein, 23 kDa, syndet) is thought to be a key player in many distinct protein trafficking events in non-neuronal cells. For example, SNAP-23 is involved in diverse protein trafficking events such as glucose transporter type 4 (GLUT-4) trafficking in adipocytes, compound exocytosis in mast cells, polarized protein trafficking, platelet dense core granule release.

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 2

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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Identification of a novel syntaxin-and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues
Ravichandran V, et al.
Test, 271(23), 13300-13303 (1996)
Primary fibroblasts from CSP alpha mutation carriers recapitulate hallmarks of the adult onset neuronal ceroid lipofuscinosis
Benitez BA and Sands MS
Scientific Reports, 7(1), 6332-6332 (2017)
Small-Interfering RNA-Mediated Identification and Regulation of the Ternary SNARE Complex Mediating RBL-2H3 Mast Cell Degranulation
Woska Jr J R and Gillespie M E
Scandinavian Journal of Immunology, 73(1), 8-17 (2011)
Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing
Ungermann C and Langosch D
Journal of Cell Science, 118(17), 3819-3828 (2005)
Sebastian Mohr et al.
Cancer cell, 31(4), 549-562 (2017-04-12)
The transcription factor Meis1 drives myeloid leukemogenesis in the context of Hox gene overexpression but is currently considered undruggable. We therefore investigated whether myeloid progenitor cells transformed by Hoxa9 and Meis1 become addicted to targetable signaling pathways. A comprehensive (phospho)proteomic analysis

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