SNAP-25

SNAP-25NCBI

SNAP-25

Crude human synaptic immunoprecipitate

This product appears to recognise the human pre-synaptic protein SNAP-25; an antigen of 26-27kD molecular weight. It will recognise SNAP-25 fusion protein from COS cells but not with the fusion protein from bacterial systems. Research studies have used this antibody to study the distribution of synaptic changes in the hippocampus of patients with medically refractory temporal lobe epilepsy. (1 3 & 8).

Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant

Immunohistology - Paraffin - 1/2000 - 1/5000 Summary: Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene. Summary: Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq]. 1. Honer. W. G. et al. (1994) Hippocampal synaptic pathology in patients with temporal lobe epilepsy. 2. Honer. W. G et al. (1992) Regional synaptic pathology in Alzheimer\' s disease. 3. Honer. W. G. et al. (1993) Human synaptic proteins with a heterogeneous distribution in cerebellum and visual cortex. 4. Honer. W. G. et al. (1992) Characterization of a synaptic antigen of interest in neuropsychiatric illness. 5. Honer. W. G. et al. (1989) Monoclonal antibodies to study the brain in schizophrenia. 6. Masliah. E. et al. (1994) Topographical distribution of synaptic-associated proteins in the neuritic plaques of Alzheimer\' s disease hippocampus. 7. Simpson. I. A. et al. (1994) Decreased concentrations of GLUT1 and GLUT3 glucose transporters in the brains of patients with Alzheimer\' s disease. 8. Wakabayashi. K. et al. (1994) Synapse alterations in the hippocampalentorhinal formation in Alzheimer\' s disease with and without Lewy body disease. 9. Dickson. D. W. et al. (1994) Hippocampal sclerosis: a common pathological feature of dementia in very old (> or = 80 years of age) humans. 10. Dickson. D. W. et al. (1995) Correlations of synaptic and pathological markers with cognition of the elderly. 11. Dickson. D. W. et al. (1995) Correlations of synaptic markers with cognitive status in prospectively studied elderly humans. Neurobiol. Aging 16: 285-98.