STX1A Human

Syntaxin-1A Human Recombinant
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Cat. No.
BT8621
Source
Escherichia Coli.
Synonyms
STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.
Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Gene and Protein Structure

  • Gene: STX1A spans ~20.42 kb, containing 10 exons and encoding a 288-amino acid protein .

  • Protein Domains:

    • N-terminal regulatory domain (Habc): Mediates interactions with regulatory proteins.

    • Central SNARE domain (H3): Forms the core of the SNARE complex.

    • C-terminal transmembrane domain: Anchors the protein to the plasma membrane .

  • Molecular Weight: ~30.7 kDa (recombinant form) .

PropertyValueSource
Gene Location7q11.23
Protein Length288 amino acids
Transmembrane DomainSingle C-terminal domain
Molecular Weight30.7 kDa (recombinant)

Core Functions

  1. SNARE Complex Assembly:

    • Forms the core of the SNAP25-STX1A-VAMP2 complex, facilitating synaptic vesicle fusion with the presynaptic membrane .

    • Regulates calcium-triggered neurotransmitter release (e.g., dopamine, serotonin) and hormone secretion (e.g., insulin, GLP-1) .

  2. Ion Channel Regulation:

    • Interacts with voltage-dependent calcium (VDCC) and potassium channels via the H3 domain .

    • Modulates acrosomal exocytosis in sperm and dense-core vesicle release in pancreatic β-cells .

  3. Neurotransmitter Release:

    • Target of botulinum neurotoxin type C, which cleaves the H3 domain to block exocytosis .

Key Findings from Human and Animal Studies

Study FocusFindingsCitation
Williams SyndromeSTX1A expression levels correlate with 15.6% of cognitive variation (n=65)
7q11.23 DuplicationSTX1A overexpression linked to pain insensitivity in humans and mice
Autism and EpilepsyMissense variants and deletions in STX1A cause intellectual disability and seizures
Cardiac FunctionSTX1A knockout in mice induces electromechanical delay and ventricular dysfunction

Mechanistic Insights

  • Williams Syndrome: Reduced STX1A expression disrupts presynaptic vesicle release, impairing synaptic plasticity and intelligence .

  • Pain Insensitivity: Overexpression in nociceptive DRG neurons reduces TRPV1-mediated calcium influx, dampening pain signaling .

  • Autism and Epilepsy: Missense variants weaken STX1A-STXBP1 interactions, leading to hyperexcitability and seizures .

Protein Characteristics and Recombinant Production

ParameterDetailSource
Recombinant ExpressionExpressed in E. coli; purified via chromatography (>95% purity)
Post-Translational ModificationsPhosphorylated by CK2; Ser-188 phosphorylation by DAPK1 reduces STXBP1 binding
StabilityStore at -20°C; avoid freeze-thaw cycles

Therapeutic and Diagnostic Potential

  • Neurological Disorders: Targeting STX1A expression or SNARE complex dynamics may treat synaptic dysfunction in autism and epilepsy .

  • Pain Management: Modulating STX1A in nociceptive neurons could offer novel analgesic strategies .

  • Cardiac Dysfunction: STX1A’s role in calcium handling underscores its relevance to arrhythmia and heart failure research .

Product Specs

Introduction
Syntaxin is a membrane-bound protein known as a Q-SNARE, which plays a crucial role in exocytosis. It comprises three main parts: an N-terminal regulatory domain (Habc), a SNARE domain (H3), and a C-terminal transmembrane domain. The SNARE (H3) domain interacts with synaptobrevin and SNAP-25 to create the core SNARE complex. During calcium-regulated exocytosis, synaptic vesicles release stored neurotransmitters. The precise release of neurotransmitters relies on the strategic positioning of both synaptic vesicles and calcium channels within the presynaptic active zone, a process facilitated by Syntaxins. Furthermore, Syntaxins act as a substrate for botulinum neurotoxin type C, a metalloprotease. This toxin effectively blocks exocytosis due to its strong affinity for a molecular complex that includes the alpha-latrotoxin receptor, a key player in exocytosis.
Description
Recombinant Human Syntaxin-1A, produced in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 226 amino acids (1-226) and has a molecular weight of 26.1 kDa. It includes both the N-terminal domain (Habc) and the t_SNARE domain (H3 domain).
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
This protein solution is prepared in a buffer consisting of 20mM Tris-HCl at pH 7.5, 10% glycerol, and 1mM DTT.
Stability
For optimal storage: - Refrigerate at 4°C if the entire vial will be used within 2-4 weeks. - For longer storage, freeze at -20°C. - Consider adding a carrier protein (0.1% HSA or BSA) for extended storage. Important: Avoid repeated freezing and thawing cycles.
Purity
High purity exceeding 95.0%, as determined by SDS-PAGE analysis.
Synonyms
STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.
Source
Escherichia Coli.
Amino Acid Sequence
MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

Product Science Overview

Structure and Expression

Syntaxin-1A is a protein composed of 265 amino acids with a molecular weight of approximately 30.7 kDa . The recombinant human Syntaxin-1A is typically expressed in Escherichia coli and purified using conventional chromatography techniques . The protein is often formulated in phosphate-buffered saline (pH 7.4) containing 10% glycerol and 1mM DTT to maintain its stability .

Function

Syntaxin-1A plays a pivotal role in the exocytosis of hormones and neurotransmitters. It is involved in the docking of synaptic vesicles at presynaptic active zones, which is a critical step in the release of neurotransmitters into the synaptic cleft . This protein is part of the SNARE (Soluble NSF Attachment Receptor) complex, which also includes SNAP25 and VAMP2. The SNARE complex mediates the fusion of synaptic vesicles with the presynaptic plasma membrane, facilitating neurotransmitter release .

In addition to its role in neurotransmitter release, Syntaxin-1A is also implicated in the calcium-dependent regulation of the acrosomal reaction in sperm . This reaction is essential for fertilization, as it allows the sperm to penetrate the egg.

Research and Applications

Recombinant human Syntaxin-1A is widely used in research to study the mechanisms of synaptic vesicle fusion and neurotransmitter release. It is also used to investigate the role of SNARE proteins in various cellular processes. Studies have shown that Syntaxin-1A is phosphorylated by CK2, and phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 .

Storage and Handling

Recombinant human Syntaxin-1A can be stored at +2°C to +8°C for short-term use (up to one week). For long-term storage, it is recommended to aliquot and store the protein at -20°C to -80°C to avoid repeated freezing and thawing cycles .

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