VAMP2 Antibody [M16L18] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:10000 - 1:50000 IP1:150 IF1:250 FCM1:100

Application
WB, IP, IF, FCM

Reactivity
Mouse, Rat, Human

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
13 kDa,36 kDa

Positive Control	Human cerebellum; Rat heart; Mouse brain; Human fetal brain; Human cerebellum; SH-SY5Y cells; Jurkat cells; U87-MG cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
VAMP2 Antibody [M16L18] detects endogenous levels of total VAMP2 protein.

Clone
M16L18

Synonym(s)
SYB2; VAMP2; Vesicle-associated membrane protein 2; VAMP-2; Synaptobrevin-2

Background
VAMP2, also known as vesicle-associated membrane protein 2 or synaptobrevin-2, is a v-SNARE protein of the SNARE superfamily that is embedded in synaptic vesicle membranes and is essential for calcium-triggered neurotransmitter release. It accomplishes this by zippering with plasma membrane t-SNAREs syntaxin-1A and SNAP-25 to form a trans-SNARE complex, which drives hemifusion and the opening of the fusion pore. VAMP2 is a protein of about 116 amino acids, featuring an intrinsically disordered N-terminal proline-rich region, a conserved 61-residue SNARE motif with key residues like glutamine 48, arginine 56, and glutamine 72 that form ionic locks, a juxtamembrane amphipathic helix, and a C-terminal transmembrane domain anchoring it to the synaptic vesicle lipid bilayer. Its conformational dynamics are regulated by cholesterol-rich lipid rafts, which release the SNARE motif for complex assembly. Within these rafts, VAMP2's SNARE motif takes on a membrane-free alpha-helical state, primed for rapid trans-SNARE zippering that generates sufficient force to overcome fusion barriers, while in non-raft regions, it binds the membrane in a helical form to prevent untimely vesicle fusion until fusion is triggered by synaptotagmin or lipid signals. VAMP2 also forms hexameric rings with synaptophysin through interactions of their cytosolic tails, clustering synaptic vesicle SNAREs for cooperative vesicle docking, priming, and ensuring the rapid exocytosis kinetics required at synapses, and it also mediates granule release in neutrophils and peptide secretion from cardiomyocytes. Disrupted VAMP2 function, such as through cleavage by botulinum neurotoxins, leads to impaired synaptic transmission, causing conditions like botulism, epilepsy, and neurodegeneration, while mutations can disturb synaptic vesicle trafficking and SNARE-mediated cooperativity.

Background

VAMP2, also known as vesicle-associated membrane protein 2 or synaptobrevin-2, is a v-SNARE protein of the SNARE superfamily that is embedded in synaptic vesicle membranes and is essential for calcium-triggered neurotransmitter release. It accomplishes this by zippering with plasma membrane t-SNAREs syntaxin-1A and SNAP-25 to form a trans-SNARE complex, which drives hemifusion and the opening of the fusion pore. VAMP2 is a protein of about 116 amino acids, featuring an intrinsically disordered N-terminal proline-rich region, a conserved 61-residue SNARE motif with key residues like glutamine 48, arginine 56, and glutamine 72 that form ionic locks, a juxtamembrane amphipathic helix, and a C-terminal transmembrane domain anchoring it to the synaptic vesicle lipid bilayer. Its conformational dynamics are regulated by cholesterol-rich lipid rafts, which release the SNARE motif for complex assembly. Within these rafts, VAMP2's SNARE motif takes on a membrane-free alpha-helical state, primed for rapid trans-SNARE zippering that generates sufficient force to overcome fusion barriers, while in non-raft regions, it binds the membrane in a helical form to prevent untimely vesicle fusion until fusion is triggered by synaptotagmin or lipid signals. VAMP2 also forms hexameric rings with synaptophysin through interactions of their cytosolic tails, clustering synaptic vesicle SNAREs for cooperative vesicle docking, priming, and ensuring the rapid exocytosis kinetics required at synapses, and it also mediates granule release in neutrophils and peptide secretion from cardiomyocytes. Disrupted VAMP2 function, such as through cleavage by botulinum neurotoxins, leads to impaired synaptic transmission, causing conditions like botulism, epilepsy, and neurodegeneration, while mutations can disturb synaptic vesicle trafficking and SNARE-mediated cooperativity.

References
https://pubmed.ncbi.nlm.nih.gov/36618823/ https://pubmed.ncbi.nlm.nih.gov/32210233/

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

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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%