VAP33 Mouse, Unlabeled, Clone: 8, BD
Mouse Monoclonal Antibody
Manufacturer: BD Biosciences 612180
In eukaryotic cells, trafficking of membrane and secretory proteins requires an elaborate system of organelles, vesicles, and cytoskeletal structures. Proteins important for protein trafficking usually interact with one or all of these cellular structures. VAP33 (VAP-A) was identified through its ability to bind the synaptic vesicle protein synaptobrevin/VAMP-1. The structure of VAP33 includes an N-terminal domain similar to the major sperm protein from Ascaris lubricoides, a central coiled-coil domain, and a C-terminal transmembrane region. VAP33 mRNA is expressed at high levels in testis, but is also found in most other tissues. In rat neurons, VAP33 localizes to the ER and microtubules, while in many cells and tissues, VAP33 co-localizes to tight junctions along with occludin. Interestingly, 83% of VAP33 fractionates with occludin and DPPIV in the plasma membrane fraction, while only 14% fractionates in the vesicular pool. In L6 skeletal myoblasts, VAP33 colocalizes with VAMP-2, and overexpression of VAP33 attenuates insulin-dependent incorporation of GLUT4 into the plasma membrane. This effect can be suppressed by overexpression of VAMP-2. Thus, VAP33 may be involved in the trafficking of plasma membrane proteins to specific sites within the cell.
Immunofluorescence, Western Blotting
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
|Store undiluted at -20°C.|
|Mouse VAP33 aa. 119-226|
|Canine, Human, Murine, Rat|
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