MAL, a nonglycosylated integral membrane proteolipid, has been identified as a major internal component of glycolipid-enriched membrane (GEM) microdomains. MAL is the first integral membrane proteolipid component to have been shown as a necessary element in the cellular apical sorting apparatus for newly synthesized proteins. In its steady state this highly hydrophobic proteolipid, resides predominantly in the apical zone of polarized epithelial cells. It has also been shown in itinerant protein cycling between the plasma membrane and endosomes and in other cells. This 17-kDa proteolipid contains four putative transmembrane domains. These domains along with its protein trafficking properties are defined by the specific signals delegated by its specific amino acid sequence.
17 kDa myelin vesicular protein; mal T-cell differentiation protein; MVP17; MyD88-adapter-like; Myelin and lymphocyte protein; myelin and lymphocyte protein, T-cell differentiation protein; NS 3; T-lymphocyte maturation-associated protein
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