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SNAP25 antibody (Synaptosomal-Associated Protein, 25kDa)

Details for Product anti-SNAP25 Antibody No. ABIN350909, Supplier: Log in to see
Antigen
  • bA416N4.2
  • Bdr
  • dJ1068F16.2
  • fj55h11
  • ric-4
  • RIC-4
  • ric4
  • RIC4
  • SEC9
  • sec9
  • SNAP
  • SNAP-25
  • snap-25
  • SNAP-25a
  • SNAP-25B
  • snap25
  • sp
  • wu:fj55h11
Reactivity
Rat (Rattus), Mouse (Murine)
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132
102
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29
21
15
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14
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2
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Host
Sheep
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143
24
6
1
Clonality
Polyclonal
Conjugate
This SNAP25 antibody is un-conjugated
12
11
9
9
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7
4
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3
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2
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2
1
1
1
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1
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1
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1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
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188
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66
47
28
18
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.
Isotype IgG
Specificity Specific for SNAP-25.
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 concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 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).

Scales, Hesser, Masuda, Scheller: "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).

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).

Coppola, Magnin-Luthi, Perret-Menoud, Gattesco, Schiavo, Regazzi: "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, Bansal, Pfeiffer: "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, Pabst, Jahn: "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, Brunger: "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, Sacks, Scheller: "Hrs-2 is an ATPase implicated in calcium-regulated secretion." in: Nature, Vol. 385, Issue 6619, pp. 826-9, 1997 (PubMed).

Jacobsson, Piehl, Bark, Zhang, Meister: "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, Skene: "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).