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VAMP2 Membrane Protein Introduction

Introduction of VAMP2

The Vesicle-associated membrane protein 2 encoded by VAMP2 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. VAMP2 is a key part of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) that is involved in synaptic vesicle exocytosis, a fundamental step in neurotransmitter release between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, and synaptotagmin. It also forms a distinct complex with synaptophysin. Besides, VAMP2 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.

Basic Information of VAMP2
Protein Name Vesicle-associated membrane protein 2 (VAMP-2)
Gene Name VAMP2
Aliases Synaptobrevin-2
Organism Homo sapiens (Human)
UniProt ID P63027
Transmembrane Times 1
Length (aa) 116
Sequence MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST

Function of VAMP2 Membrane Protein

VAMP2 plays a crucial role in membrane fusion, mediating protein trafficking and the secretion of physiological mediators. Except that, the VAMP2 plays vital roles in other processes. VAMP2 can function as a molecular marker for both quiescent satellite cells and myotubes, but not for proliferating myoblasts. Thyroid hormone may promote glucose uptake via enhancing insulin-induced phosphorylation of Akt and subsequent translocations of VAMP2 and GLUT4 in 3T3-L1 adipocytes. Additionally, by reducing VAMP2 expression in a murine model of epilepsy, mice showed significant reductions in potassium-evoked glutamate release, which leads to a kindling-resistant phenotype. Because VAMP2 gene encodes a synaptic vesicle protein and its special map location, it may play role in the pathogenesis of Familial Infantile Myasthenia Gravis (FIMG).

A model for tethering and fusion of Tfn-TfnR-containing recycling vesicles with the PM, mediated by Rab11, the exocyst and SNAREs. Fig.1 A model for tethering and fusion of Tfn-TfnR-containing recycling vesicles with the PM, mediated by Rab11, the exocyst and SNAREs. (Kubo, 2015)

Application of VAMP2 Membrane Protein in Literature

  1. Caceres P.S., et al. Vesicle-associated membrane protein 2 (VAMP2) but Not VAMP3 mediates cAMP-stimulated trafficking of the renal Na⁺-K⁺-2Cl⁻ -co-transporter NKCC2 in thick ascending limbs. Journal of Biological Chemistry. 2014, 289(34):23951-62. PubMed ID: 25008321

    This article finds that cAMP stimulation enhances VAMP2 exocytosis and promotes VAMP2 interaction with NKCC2.

  2. Jung Y., et al. VAMP2-NRG1 Fusion Gene is a Novel Oncogenic Driver of Non-Small-Cell Lung Adenocarcinoma. Journal of Thoracic Oncology. 2015, 10(7):1107-11. PubMed ID: 26134228

    This article suggests that VAMP2-NRG1 fusion gene, in particular, its most dominant splice variant, is capable of promoting cellular growth and thus likely functions as an oncogene.

  3. Manca P., et al. Distribution of SNAP25, VAMP1 and VAMP2 in mature and developing deep cerebellar nuclei after estrogen administration. Neuroscience. 2014, 266:102-15. PubMed ID: 24534378

    This article suggests that the distribution of SNAP25, VAMP1 and VAMP2 is age-related and submitted to estrogenic control during development. Changes in SNAP25, VAMP1 and VAMP2 in defined nerve terminals could correlate with alterations of specific synaptic properties.

  4. Koo S.J., et al. Vesicular Synaptobrevin/VAMP2 Levels Guarded by AP180 Control Efficient Neurotransmission. Neuron. 2015, 88(2):330-44. PubMed ID: 26412491

    This article reveals an essential role for AP180-mediated high-fidelity sorting of Syb2 in SV reformation and neurotransmission.

  5. Hu S., et al. MicroRNA-34c Downregulation Ameliorates Amyloid-β-Induced Synaptic Failure and Memory Deficits by Targeting VAMP2. Journal of Alzheimers Disease. 2015, 48(3):673-86. PubMed ID: 26402112

    This article suggests that the Aβ-miR-34cVAMP2 pathway partially explains the mechanism underlying VAMP2 reduction in AD patients.

VAMP2 Preparation Options

Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-VAMP2 antibody development services.


During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

Reference

  1. Kubo K, et al. (2015). SNAP23/25 and VAMP2 mediate exocytic event of transferrin receptor-containing recycling vesicles. Biology Open. 4(7): 910-20.

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