SNAP25 Antibody [P1D7] | Primary Antibodies

Application: Reactivity: Mouse, Human, Rat

Lane 1: Mouse brain, Lane 2: Rat brain

Usage Information

Dilution
WB1:1000 IF1:1250 FCM1:200

Application
WB, IF, FCM

Reactivity
Mouse, Human, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
23 kDa 27 kDa, 25 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
SNAP25 Antibody [P1D7] detects endogenous levels of total SNAP25 protein.

Clone
P1D7

Synonym(s)
SNAP, SNAP25, Synaptosomal-associated protein 25, SNAP-25, Super protein, Synaptosomal-associated 25 kDa protein, SUP

Background
SNAP25 (synaptosomal‑associated protein 25) is a neuron‑enriched t‑SNARE of the synaptobrevin–syntaxin–SNAP25 family that anchors on the presynaptic plasma membrane and provides two of the four α‑helices in the core SNARE bundle that drives fast Ca²⁺‑regulated exocytosis of synaptic vesicles and other secretory organelles. The protein contains two SNARE motifs separated by a flexible linker and lacks a transmembrane domain; palmitoylation of clustered cysteines in the central region targets SNAP25 to cholesterol‑rich domains of the presynaptic membrane where it assembles with syntaxin‑1 and vesicular synaptobrevin/VAMP2 into a parallel four‑helix bundle that bridges vesicle and plasma membranes and supplies the energy for membrane merger. Within this fusion machinery, SNAP25 functions as a central organizing platform that not only contributes half of the helical core but also binds regulatory factors such as synaptotagmin, complexins, Munc18 and Munc13, and scaffolding proteins that define release probability, vesicle priming, and coupling of SNARE zippering to Ca²⁺ sensing. The C‑terminal SNARE motif of SNAP25 contains defined interfaces for synaptotagmin‑1 and synaptotagmin‑7, and targeted alterations within these interfaces shift the balance between vesicle docking, priming, and fusion, indicating that SNAP25–synaptotagmin contacts position Ca²⁺ sensors at sites where partially zippered SNARE complexes await Ca²⁺ influx to trigger final fusion. SNAP25 participates in multiple exocytotic pathways, including fast synchronous synaptic vesicle release, asynchronous and spontaneous neurotransmitter release, and dense‑core vesicle fusion for neuropeptide secretion, where its presence or partial functional replacement by homologs such as SNAP23 and SNAP29 defines the efficiency and developmental timing of these secretory events. Expression is highest in neurons of the central nervous system, with SNAP25a and SNAP25b splice isoforms showing developmentally regulated patterns that correlate with maturation of synaptic transmission and plasticity; switching from the a to the b isoform refines short‑term plasticity and release kinetics without changing the basic SNARE architecture. At the pathway level, SNAP25 integrates into the neurotransmitter release cycle, with phosphorylation by kinases such as PKA and PKC, palmitoylation turnover, and interactions with Ca²⁺ channels and K⁺ channels shaping vesicle pool dynamics, presynaptic excitability, and coupling between action potentials and exocytosis. Disease‑linked missense variants in SNAP25 cluster in regions that contact synaptotagmin and other SNAREs, change the energy landscape of SNARE complex assembly, reduce vesicle priming, and alter spontaneous versus evoked release, and these mechanistic defects associate with epileptic encephalopathy, intellectual disability, and movement or neurodevelopmental disorders.

Background

SNAP25 (synaptosomal‑associated protein 25) is a neuron‑enriched t‑SNARE of the synaptobrevin–syntaxin–SNAP25 family that anchors on the presynaptic plasma membrane and provides two of the four α‑helices in the core SNARE bundle that drives fast Ca²⁺‑regulated exocytosis of synaptic vesicles and other secretory organelles. The protein contains two SNARE motifs separated by a flexible linker and lacks a transmembrane domain; palmitoylation of clustered cysteines in the central region targets SNAP25 to cholesterol‑rich domains of the presynaptic membrane where it assembles with syntaxin‑1 and vesicular synaptobrevin/VAMP2 into a parallel four‑helix bundle that bridges vesicle and plasma membranes and supplies the energy for membrane merger. Within this fusion machinery, SNAP25 functions as a central organizing platform that not only contributes half of the helical core but also binds regulatory factors such as synaptotagmin, complexins, Munc18 and Munc13, and scaffolding proteins that define release probability, vesicle priming, and coupling of SNARE zippering to Ca²⁺ sensing. The C‑terminal SNARE motif of SNAP25 contains defined interfaces for synaptotagmin‑1 and synaptotagmin‑7, and targeted alterations within these interfaces shift the balance between vesicle docking, priming, and fusion, indicating that SNAP25–synaptotagmin contacts position Ca²⁺ sensors at sites where partially zippered SNARE complexes await Ca²⁺ influx to trigger final fusion. SNAP25 participates in multiple exocytotic pathways, including fast synchronous synaptic vesicle release, asynchronous and spontaneous neurotransmitter release, and dense‑core vesicle fusion for neuropeptide secretion, where its presence or partial functional replacement by homologs such as SNAP23 and SNAP29 defines the efficiency and developmental timing of these secretory events. Expression is highest in neurons of the central nervous system, with SNAP25a and SNAP25b splice isoforms showing developmentally regulated patterns that correlate with maturation of synaptic transmission and plasticity; switching from the a to the b isoform refines short‑term plasticity and release kinetics without changing the basic SNARE architecture. At the pathway level, SNAP25 integrates into the neurotransmitter release cycle, with phosphorylation by kinases such as PKA and PKC, palmitoylation turnover, and interactions with Ca²⁺ channels and K⁺ channels shaping vesicle pool dynamics, presynaptic excitability, and coupling between action potentials and exocytosis. Disease‑linked missense variants in SNAP25 cluster in regions that contact synaptotagmin and other SNAREs, change the energy landscape of SNARE complex assembly, reduce vesicle priming, and alter spontaneous versus evoked release, and these mechanistic defects associate with epileptic encephalopathy, intellectual disability, and movement or neurodevelopmental disorders.

References
https://pubmed.ncbi.nlm.nih.gov/24005294/ https://pubmed.ncbi.nlm.nih.gov/27047369/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%