Syntaxin Antibody [K5F22] | Primary Antibodies

Application: Reactivity: Human, Rat

Usage Information

Dilution
WB1:1000 IF1:50

Application
WB, IF

Reactivity
Human, Rat

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 Observed MW
33 kDa 35 kDa, 48 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
Syntaxin Antibody [K5F22] detects endogenous levels of total Syntaxin protein.

Clone
K5F22

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

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

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

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%