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SNAP25 antibody (Synaptosomal-Associated Protein, 25kDa)

Details for Product anti-SNAP25 Antibody No. ABIN350908, Supplier: Log in to see
Antigen
  • ric-4
  • ric4
  • sec9
  • snap-25
  • SNAP-25B
  • SNAP-25a
  • Bdr
  • SNAP-25
  • sp
  • RIC-4
  • RIC4
  • SEC9
  • SNAP
  • bA416N4.2
  • dJ1068F16.2
  • fj55h11
  • snap25
  • wu:fj55h11
Reactivity
Rat (Rattus), Mouse (Murine)
264
108
99
31
21
15
15
14
10
8
5
4
3
3
2
2
2
1
1
1
1
Host
Sheep
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128
23
6
1
Clonality
Polyclonal
Conjugate
This SNAP25 antibody is un-conjugated
9
8
6
6
6
6
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
227
149
92
64
45
45
27
17
15
11
11
8
2
2
2
1
Supplier
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Immunogen A synthetic peptide from mouse Synaptosomal-associated protein 25 (SNAP-25, SNAP25, SEC9, RIC-4) conjugated to an immunogenic carrier protein was used as the antigen.
Specificity Specific for SNAP-25.
Purification Whole serum
Alternative Name SNAP-25 (SNAP25 Antibody Abstract)
Background Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion.
Subunit: Part of the SNARE core complex containingSNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1,SNAP25BP and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8. Found in a complex containing SYT1, SV2B and syntaxin-1.
Subcellular location: Membrane, Lipid-anchor. Cell junction, synapse, synaptosome. Note: Membrane association requires palmitoylation.
Tissue specificity: Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum. Also known as:SNAP-25, Synaptosomal-associated 25 kDa protein,SNAP25, RIC4, SEC9,SNAP, RIC-4, Super protein, SUP.
Application Notes A dilution of 1 : 300 to 1 :2000 is recommended.
The optimal dilution should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 500 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Ernst, Brunger: "High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex." in: The Journal of biological chemistry, Vol. 278, Issue 10, pp. 8630-6, 2003 (PubMed).

Hepp, Cabaniols, Roche: "Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A." in: FEBS letters, Vol. 532, Issue 1-2, pp. 52-6, 2002 (PubMed).

Scales, Hesser, Masuda et al.: "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly." in: The Journal of biological chemistry, Vol. 277, Issue 31, pp. 28271-9, 2002 (PubMed).

Coppola, Magnin-Luthi, Perret-Menoud et al.: "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin." in: The Journal of biological chemistry, Vol. 276, Issue 35, pp. 32756-62, 2001 (PubMed).

Bouverat, Krueger, Coetzee et al.: "Expression of rab GTP-binding proteins during oligodendrocyte differentiation in culture." in: Journal of neuroscience research, Vol. 59, Issue 3, pp. 446-53, 2000 (PubMed).

Fasshauer, Antonin, Margittai et al.: "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties." in: The Journal of biological chemistry, Vol. 274, Issue 22, pp. 15440-6, 1999 (PubMed).

Sutton, Fasshauer, Jahn et al.: "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution." in: Nature, Vol. 395, Issue 6700, pp. 347-53, 1998 (PubMed).

Bean, Seifert, Chen et al.: "Hrs-2 is an ATPase implicated in calcium-regulated secretion." in: Nature, Vol. 385, Issue 6619, pp. 826-9, 1997 (PubMed).

Jacobsson, Piehl, Bark et al.: "Differential subcellular localization of SNAP-25a and SNAP-25b RNA transcripts in spinal motoneurons and plasticity in expression after nerve injury." in: Brain research. Molecular brain research, Vol. 37, Issue 1-2, pp. 49-62, 1996 (PubMed).

Hess, Slater, Wilson et al.: "The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 12, Issue 12, pp. 4634-41, 1993 (PubMed).