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Recombinant Human Vesicle-associated membrane protein 2 (VAMP2)

The N-terminal GST-tagged recombinant vesicle-associated membrane protein 2 (VAMP2) is produced by expressing the target gene fragment in E.coli and fusing the GST tag to the N-terminus of the resulting protein. The target gene sequence corresponds to the intact amino acids of the human VAMP2. Its purity is greater than 90% determined by SDS-PAGE. On the gel, this recombinant VAMP2 protein migrated to the molecular weight band of approximately 40 kDa. It has also been validated its component by the LC-MS/MS analysis. The target protein VAMP2 is involved in several biological processes, including the targeting or fusion of transport vesicles to their target membrane and the insulin-regulated trafficking of GLUT4 in adipocytes.

ACP03776

The N-terminal GST-tagged recombinant vesicle-associated membrane protein 2 (VAMP2) is produced by expressing the target gene fragment in E.coli and fusing the GST tag to the N-terminus of the resulting protein. The target gene sequence corresponds to the intact amino acids of the human VAMP2. Its purity is greater than 90% determined by SDS-PAGE. On the gel, this recombinant VAMP2 protein migrated to the molecular weight band of approximately 40 kDa. It has also been validated its component by the LC-MS/MS analysis. The target protein VAMP2 is involved in several biological processes, including the targeting or fusion of transport vesicles to their target membrane and the insulin-regulated trafficking of GLUT4 in adipocytes.

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Specifications


Cat.No ACP03776 Target NameVAMP2
FormLiquid or Lyophilized powderExpression SystemE.coli
Expression Range1-116aaMol Weight40.1 kDa
Protein LengthFull lengthPurityGreater than 90% as determined by SDS-PAGE.
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDP63027
Background Information
  • Uniprot Id

    P63027

  • Target Species

    Human

  • Target Name

    VAMP2

  • Target Full Name

    Vesicle-associated membrane protein 2

  • Target Function

    Involved in the targeting and/or fusion of transport vesicles to their target membrane. Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.

  • Target Subcellular Location

    Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell membrane.

  • Target Protein Families

    Synaptobrevin family

  • Target Tissue Specificity

    Nervous system and skeletal muscle.

  • Target Research Area

    Cancer

  • Target Synonyms

    FLJ11460; RATVAMPB; RATVAMPIR; SYB; SYB2; Synaptobrevin 2; Synaptobrevin-2; VAMP 2; VAMP-2; Vamp2; VAMP2_HUMAN; Vesicle associated membrane protein 2; Vesicle-associated membrane protein 2 (synaptobrevin 2); Vesicle-associated membrane protein 2

  • Target Background

    The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. It is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG.

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