Syntaxin Antibody [K5F22] Datasheet

Biological Description

Specificity	Syntaxin Antibody [K5F22] detects endogenous levels of total Syntaxin protein.
Background	Syntaxin proteins, prototypical t-SNAREs of the SNARE superfamily, anchor to target membranes via C-terminal transmembrane domains and mediate docking and fusion specificity across eukaryotic vesicular transport pathways from the ER to the plasma membrane. Characteristic structural elements include a membrane-proximal SNARE motif forming coiled-coil helices for parallel four-helix bundle assembly and an N-terminal Habc domain composed of three α-helices that folds back onto the SNARE motif to enforce a closed, autoinhibited conformation. In this closed state, Munc18 binds tightly to stabilize inactivity and prevent premature SNARE interactions; upon priming by Munc13 or synaptotagmin-Ca2+ signals, the Habc domain unfolds to the open state. This transition enables the syntaxin SNARE motif to zipper with SNAP-25 and the v-SNARE VAMP2 into trans-SNARE complexes that bridge vesicle and plasma membranes, culminating in hemifusion and full fusion driven by NSF/α-SNAP disassembly. Syntaxin-1 isoforms predominate in neuronal presynaptic terminals for fast neurotransmitter release, while syntaxin-4 drives GLUT4 translocation and syntaxin-5 facilitates ER-Golgi anterograde traffic. Direct interactions with voltage-gated ion channels localize fusion sites, while Rab effectors and synaptotagmin sense calcium to accelerate the zippering process. Mutations or proteolytic cleavage by botulinum neurotoxin C truncate syntaxin-1, blocking SNARE assembly and inducing plasma membrane recycling defects, which contributes to neuronal degeneration and synaptic loss in conditions such as botulism and Alzheimer’s disease.

Specificity

Syntaxin Antibody [K5F22] detects endogenous levels of total Syntaxin protein.

Background

Syntaxin proteins, prototypical t-SNAREs of the SNARE superfamily, anchor to target membranes via C-terminal transmembrane domains and mediate docking and fusion specificity across eukaryotic vesicular transport pathways from the ER to the plasma membrane. Characteristic structural elements include a membrane-proximal SNARE motif forming coiled-coil helices for parallel four-helix bundle assembly and an N-terminal Habc domain composed of three α-helices that folds back onto the SNARE motif to enforce a closed, autoinhibited conformation. In this closed state, Munc18 binds tightly to stabilize inactivity and prevent premature SNARE interactions; upon priming by Munc13 or synaptotagmin-Ca2+ signals, the Habc domain unfolds to the open state. This transition enables the syntaxin SNARE motif to zipper with SNAP-25 and the v-SNARE VAMP2 into trans-SNARE complexes that bridge vesicle and plasma membranes, culminating in hemifusion and full fusion driven by NSF/α-SNAP disassembly. Syntaxin-1 isoforms predominate in neuronal presynaptic terminals for fast neurotransmitter release, while syntaxin-4 drives GLUT4 translocation and syntaxin-5 facilitates ER-Golgi anterograde traffic. Direct interactions with voltage-gated ion channels localize fusion sites, while Rab effectors and synaptotagmin sense calcium to accelerate the zippering process. Mutations or proteolytic cleavage by botulinum neurotoxin C truncate syntaxin-1, blocking SNARE assembly and inducing plasma membrane recycling defects, which contributes to neuronal degeneration and synaptic loss in conditions such as botulism and Alzheimer’s disease.

Usage Information

Application

WB, IF

Dilution

WB	IF
1:1000	1:50

Reactivity

Human, Rat

Source

Mouse Monoclonal Antibody

MW

33 kDa

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

References

https://pubmed.ncbi.nlm.nih.gov/11737951/
https://pubmed.ncbi.nlm.nih.gov/18703708/

Syntaxin Antibody [K5F22]

Biological Description

Usage Information

References

Application Data