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Documenti fondamentali

S2194

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Sinonimo/i:

Anti-Synaptosomal-Associated Protein 23

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About This Item

Numero MDL:
Codice UNSPSC:
12352203

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen 23 kDa

Reattività contro le specie

mouse, rat

tecniche

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

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

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

Descrizione generale

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.

Immunogeno

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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)
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)
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
Bruno A Benitez et al.
Scientific reports, 7(1), 6332-6332 (2017-07-26)
Mutations in the co- chaperone protein, CSPα, cause an autosomal dominant, adult-neuronal ceroid lipofuscinosis (AD-ANCL). The current understanding of CSPα function exclusively at the synapse fails to explain the autophagy-lysosome pathway (ALP) dysfunction in cells from AD-ANCL patients. Here, we

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