Syntaxin1A Antibody [B3L13] | Primary Antibodies

Application: Reactivity: Human, Rat, Mouse, Mammals, Chicken

Usage Information

Dilution
WB1 : 1000 - 1 : 10000 IHC1 : 500

Application
WB, IP, IHC

Reactivity
Human, Rat, Mouse, Mammals, Chicken

Source
Mouse 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
33 kDa

Datasheet & SDS

Biological Description

Specificity
Syntaxin1A Antibody [B3L13] detects endogenous levels of total Syntaxin1A protein.

Clone
B3L13

Synonym(s)
Syntaxin-1A, Neuron-specific antigen HPC-1, STX1A, STX1

Background
Syntaxin‑1A (STX1A) is a neuronal plasma‑membrane Q‑SNARE of the syntaxin family that serves as a central organizer of fast, Ca²⁺‑triggered exocytosis by coupling synaptic vesicle docking and priming to the final membrane fusion reaction at presynaptic active zones. The protein has a tripartite architecture with an N‑terminal regulatory Habc domain forming a three‑helix bundle, a central SNARE helix (H3) that contributes the Qᴀ helix to the four‑helix neuronal SNARE complex, and a C‑terminal transmembrane segment that anchors syntaxin‑1A in the plasma membrane, while a short N‑terminal peptide and the Habc bundle together create multiple interfaces for high‑affinity binding to the SM family protein Munc18‑1. Syntaxin‑1A interconverts between a closed conformation, in which the Habc bundle folds back onto the H3 helix and masks the SNARE‑binding surface, and an open conformation, in which the H3 helix is exposed and available for SNARE complex assembly with vesicular synaptobrevin‑2 (VAMP2) and plasma‑membrane SNAP‑25; both conformations form discrete complexes with Munc18‑1, with closed syntaxin‑1A–Munc18‑1 stabilizing syntaxin at the membrane and open syntaxin‑1A–Munc18‑1 participating in assembly of fusion‑competent trans‑SNARE complexes. The conformational switch of syntaxin‑1A is a key checkpoint for synaptic vesicle fusion: enforcing the open state accelerates evoked neurotransmitter release but reduces vesicle priming capacity, while favoring the closed state stabilizes syntaxin‑1A and constrains SNARE complex formation, defining syntaxin‑1A as a molecular gate that sets both the size and release probability of the readily releasable pool. Functional regulation of syntaxin‑1A in neuroendocrine and neuronal cells involves a network of binding partners and post‑translational modifications: tomosyn and complexin bind and modulate SNARE assembly, Munc13 promotes opening and SNARE nucleation, synaptotagmin‑1 couples Ca²⁺ binding to final zippering of the SNARE bundle, and phosphorylation or palmitoylation of syntaxin‑1A or its partners tunes its interaction strength, clustering within cholesterol‑rich microdomains, and ability to support tonic versus phasic exocytosis. Syntaxin‑1A also interacts directly with presynaptic Ca²⁺ and K⁺ channels and several neurotransmitter transporters, positioning exocytotic vesicles near Ca²⁺ entry sites and modulating channel and transporter activity, which integrates vesicle fusion with presynaptic excitability and transmitter clearance. Beyond classical synapses, syntaxin‑1A contributes to hormone and peptide release from neuroendocrine cells, and emerging data indicate additional roles in lysosome exocytosis and melanosome biogenesis, extending its SNARE‑based fusion function to multiple secretory and endolysosomal pathways. Human genetic and expression data link STX1A to neurodevelopmental and neuropsychiatric “synaptopathies,” including autism spectrum conditions, epilepsy, and cognitive phenotypes, where altered syntaxin‑1A dosage or sequence can disturb SNARE coupling, short‑term plasticity, and network stability.

Background

Syntaxin‑1A (STX1A) is a neuronal plasma‑membrane Q‑SNARE of the syntaxin family that serves as a central organizer of fast, Ca²⁺‑triggered exocytosis by coupling synaptic vesicle docking and priming to the final membrane fusion reaction at presynaptic active zones. The protein has a tripartite architecture with an N‑terminal regulatory Habc domain forming a three‑helix bundle, a central SNARE helix (H3) that contributes the Qᴀ helix to the four‑helix neuronal SNARE complex, and a C‑terminal transmembrane segment that anchors syntaxin‑1A in the plasma membrane, while a short N‑terminal peptide and the Habc bundle together create multiple interfaces for high‑affinity binding to the SM family protein Munc18‑1. Syntaxin‑1A interconverts between a closed conformation, in which the Habc bundle folds back onto the H3 helix and masks the SNARE‑binding surface, and an open conformation, in which the H3 helix is exposed and available for SNARE complex assembly with vesicular synaptobrevin‑2 (VAMP2) and plasma‑membrane SNAP‑25; both conformations form discrete complexes with Munc18‑1, with closed syntaxin‑1A–Munc18‑1 stabilizing syntaxin at the membrane and open syntaxin‑1A–Munc18‑1 participating in assembly of fusion‑competent trans‑SNARE complexes. The conformational switch of syntaxin‑1A is a key checkpoint for synaptic vesicle fusion: enforcing the open state accelerates evoked neurotransmitter release but reduces vesicle priming capacity, while favoring the closed state stabilizes syntaxin‑1A and constrains SNARE complex formation, defining syntaxin‑1A as a molecular gate that sets both the size and release probability of the readily releasable pool. Functional regulation of syntaxin‑1A in neuroendocrine and neuronal cells involves a network of binding partners and post‑translational modifications: tomosyn and complexin bind and modulate SNARE assembly, Munc13 promotes opening and SNARE nucleation, synaptotagmin‑1 couples Ca²⁺ binding to final zippering of the SNARE bundle, and phosphorylation or palmitoylation of syntaxin‑1A or its partners tunes its interaction strength, clustering within cholesterol‑rich microdomains, and ability to support tonic versus phasic exocytosis. Syntaxin‑1A also interacts directly with presynaptic Ca²⁺ and K⁺ channels and several neurotransmitter transporters, positioning exocytotic vesicles near Ca²⁺ entry sites and modulating channel and transporter activity, which integrates vesicle fusion with presynaptic excitability and transmitter clearance. Beyond classical synapses, syntaxin‑1A contributes to hormone and peptide release from neuroendocrine cells, and emerging data indicate additional roles in lysosome exocytosis and melanosome biogenesis, extending its SNARE‑based fusion function to multiple secretory and endolysosomal pathways. Human genetic and expression data link STX1A to neurodevelopmental and neuropsychiatric “synaptopathies,” including autism spectrum conditions, epilepsy, and cognitive phenotypes, where altered syntaxin‑1A dosage or sequence can disturb SNARE coupling, short‑term plasticity, and network stability.

References
https://pubmed.ncbi.nlm.nih.gov/18703708/ https://pubmed.ncbi.nlm.nih.gov/36742381/

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%