SNAP-25 antibody | SP12
Mouse anti Human SNAP-25 antibody, clone SP12 has been used to study the distribution of synaptic changes in the hippocampus of patients with medically refractory temporal lobe epilepsy. (Honer et al. 1994).
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Hamster Pig Rat Gerbil
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide
- Carrier Free
- Crude human synaptic immunoprecipitate.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice were fused with cells of the NSO myeloma cell line.
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 18 months from date of despatch.
- P60880 Related reagents
- Entrez Gene
- SNAP25 Related reagents
- For research purposes only
Applications of SNAP-25 antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Paraffin||1/2000||1/5000|
- This product does not require protein digestion pre-treatment of paraffin sections. This product does not require antigen retrieval using heat treatment prior to staining of paraffin sections.
- Histology Positive Control Tissue
Secondary Antibodies Available
Product Specific References
References for SNAP-25 antibody
Honer, W.G. et al. (1994) Hippocampal synaptic pathology in patients with temporal lobe epilepsy.
Acta Neuropathol. 87 (2): 202-10.
Honer, W.G. et al. (1992) Regional synaptic pathology in Alzheimer's disease.
Neurobiol Aging. 13 (3): 375-82.
Honer, W.G. et al. (1993) Human synaptic proteins with a heterogeneous distribution in cerebellum and visual cortex.
Brain Res. 609 (1-2): 9-20.
Honer, W.G. et al. (1992) Characterization of a synaptic antigen of interest in neuropsychiatric illness.
Biol Psychiatry. 31 (2): 147-58.
Honer, W.G. et al. (1989) Monoclonal antibodies to study the brain in schizophrenia.
Brain Res. 500 (1-2): 379-83.
Masliah, E. et al. (1994) Topographical distribution of synaptic-associated proteins in the neuritic plaques of Alzheimer's disease hippocampus.
Acta Neuropathol. 87 (2): 135-42.
Simpson, I.A. et al. (1994) Decreased concentrations of GLUT1 and GLUT3 glucose transporters in the brains of patients with Alzheimer's disease.
Ann Neurol. 35 (5): 546-51.
Wakabayashi, K. et al. (1994) Synapse alterations in the hippocampal-entorhinal formation in Alzheimer's disease with and without Lewy body disease.
Brain Res. 667 (1): 24-32.
Dickson, D.W. et al. (1994) Hippocampal sclerosis: a common pathological feature of dementia in very old (≥80 years of age) humans.
Acta Neuropathol. 88 (3): 212-21.
Dickson, D.W. et al. (1995) Correlations of synaptic and pathological markers with cognition of the elderly.
Neurobiol Aging. 16 (3): 285-98; discussion 298-304.
Bragina, L. et al. (2006) GLT-1 down-regulation induced by clozapine in rat frontal cortex is associated with synaptophysin up-regulation.
J Neurochem. 99: 134-41.
Steel, G.J. et al. (1997) Evidence for interaction of the fusion protein alpha-SNAP with membrane lipid.
Biochem J. 325 : 511-8.
Reed, G.L. et al. (1999) Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion.
Blood. 93: 2617-26.
Vannucchi, M.G. et al. (2000) Synapse formation during neuron differentiation: an in situ study of the myenteric plexus during murine embryonic life.
J Comp Neurol. 425: 369-81.
Lemons, P.P. et al. (1997) Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery.
Blood. 90: 1490-500.
Mukaetova-Ladinska, E.B. et al. (2000) Staging of cytoskeletal and beta-amyloid changes in human isocortex reveals biphasic synaptic protein response during progression of Alzheimer's disease.
Am J Pathol. 157: 623-36.
Sawada, K. et al. (2002) Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness.
Mol Psychiatry. 7: 484-92.
Chen, H.Y. et al. (2009) Melatonin improves presynaptic protein, SNAP-25, expression and dendritic spine density and enhances functional and electrophysiological recovery following transient focal cerebral ischemia in rats.
J Pineal Res. 47: 260-70.
Ishimaru, H. et al. (2001) Changes in presynaptic proteins, SNAP-25 and synaptophysin, in the hippocampal CA1 area in ischemic gerbils.
Brain Res. 903: 94-101.