|VAMP‑1 in Mouse Spinal Cord. VAMP‑1 was detected in perfusion fixed frozen sections of mouse spinal cord using 1.7 µg/mL Goat Anti-Human/Mouse VAMP‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4828) overnight at 4 °C. Tissue was stained with the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained (green). View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.|
|Detection of Human/Mouse VAMP‑1 by Western Blot. Western blot shows lysates of human heart and brain tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse VAMP‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4828) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for VAMP‑1 at approximately 17 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
VAMP-1 (vesicle-associated membrane protein 1; also synaptobrevin-1/SYB1) is an 18 kDa member of the synaptobrevin family of proteins. It is expressed in neurons, neutrophils, and skeletal muscle cells, and participates in vesicle fusion with the plasma membrane. Human VAMP-1 is 118 amino acids (aa) in length. It is a type IV transmembrane protein that contains an N-terminal cytoplasmic region (aa 1-96) and a 22 aa transmembrane domain (aa 97-118). There is one coiled-coil region between aa 33-93. Multiple splice variants are known that show two, three, four and 81 aa substitutions for the C-terminal five amino acids. One three aa variant creates a mitochondrial targeting motif. Over aa 1-96, human VAMP-1 is 98% aa identical to mouse VAMP-1.
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