VAP33 Pure 8/VAP33 50ug

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.

1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.

2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.

3.This antibody has been developed and certified for the bioimaging application. However, a routine bioimaging test is not performed on every lot. Researchers are encouraged to titrate the reagent for optimal performance.