Synaptosomal-associated protein 25, also known as Super protein, Synaptosomal-associated 25 kDa protein, SNAP25 and SNAP, is a cytoplasm and cell membrane protein that belongs to the SNAP-25 family. SNAP25 / SUP contains 2 t-SNARE coiled-coil homology domains. SNAP25 / SUP is a membrane bound protein anchored to the cytosolic face of membranes via palmitoyl side chains in the middle of the molecule. SNAP25 / SUP protein is a component of the SNARE complex, which is proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP25 / SUP is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin. SNAP25 / SUP is involved in the molecular regulation of neurotransmitter release. It may play an important role in the synaptic function of specific neuronal systems. SNAP25 / SUP associates with proteins involved in vesicle docking and membrane fusion. SNAP25 / SUP regulates plasma membrane recycling through its interaction with CENPF. SNAP25 / SUP inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion. In glutamatergic synapses SNAP25 / SUP decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.
Post-translational: Palmitoylated (PubMed:28757145). Cys-85 appears to be the main site, and palmitoylation is required for membrane association (By similarity). (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198 bond and inhibits neurotransmitter release (PubMed:15592454, PubMed:9886085). (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type C (BoNT/C) which hydrolyzes the 198-Arg-|-Ala-199 bond and inhibits neurotransmitter release (PubMed:17718519, PubMed:9886085). C.botulinum type C only rarely infects humans. (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond and inhibits neurotransmitter release (PubMed:9886085).
生物活性
Immobilized Recombinant Human SNAP25 Protein (rp214497) at 1.0 μg/mL can bind Recombinant SNAP25 Antibody (Ab128454) with the EC50 of 19.2 ng/mL.
26.2 kDa, under reducing conditions; 26.7 & 55.5 & 92.9 & 133.3 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
冻干(Lyophilized)
储存缓冲液
Lyophilized from PBS, pH 7.4.
浓度
见COA
复溶
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 1.0 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
-20℃保存 12个月；复溶后建议分装，避免反复冻融。
图片
Recombinant Human SNAP25 Protein (rp214497) - ELISA
Immobilized Recombinant Human SNAP25 Protein (rp214497) at 1.0 μg/mL can bind Recombinant SNAP25 Antibody (Ab128454) with the EC₅₀ of 19.2 ng/mL.
Recombinant Human SNAP25 Protein (rp214497) - SDS-PAGE
3 μg/lane of Recombinant Human SNAP25 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the bands at 26.2 kDa under reducing conditions and 26.7 & 55.5 & 92.9 & 133.3 kDa under non-reducing conditions.
SNAP-25 itself has a strong self-assembly (dimerization) tendency, and the N-terminal and C-terminal coiled helical domains of SNAP-25 can also combine with each other to form homologous dimers (PMID: 9671503) .
ZJ26F0232348
危险品化学品经营许可证（带存储）