| Product Name | SNAPAP, 1-136aa, Human, Recombinant |
|---|---|
| Description | SNAPAP (SNAP associated protein) was enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPAP is an important component of the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin, which is a component of the SNARE complex that is required for synaptic vesicle docking and fusion. Recombinant human SNAPAP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | SNAPIN, SNAP25BP, SNAPAP, SNAP associated protein, SNAP associated protein SNARE associated protein snapin, Synaptosomal associated protein 25 binding protein |
| Host | E. coli |
| Molecular Weight | 34.3 kDa (300 aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 25 mM Tris-HCl, pH 7.5, 2 mM beta-mercaptoethanol, 1 mM EDTA. 1mMDTT, 20%Glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Ilardi JM., et al. (1999). Nat Neurosci. 2(2):119-124 Chheda MG., et al. (2001). Nat Cell Bioli. 3(4):331-8 |
| Background | SNAPAP (SNAP associated protein) was enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPAP is an important component of the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin, which is a component of the SNARE complex that is required for synaptic vesicle docking and fusion. Recombinant human SNAPAP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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