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Key Documents

S2194

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-Synaptosomal-Associated Protein 23

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About This Item

Numéro MDL:
Code UNSPSC :
12352203

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 23 kDa

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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