Syntaxin-6 is characterized by a single-pass type IV membrane protein structure and contains a t-SNARE coiled-coil homology domain . It is predominantly localized in the trans-Golgi network and endosomes, where it plays a pivotal role in the sorting and transport of proteins . The protein is also found in the plasma membrane, contributing to its diverse functional roles within the cell .
The primary function of Syntaxin-6 involves the regulation of intracellular vesicle trafficking. It interacts with other SNARE proteins, such as STX12, VAMP4, and VTI1A, to form a complex that facilitates the fusion of vesicles with target membranes . This interaction is essential for the proper delivery of cargo proteins to their designated locations within the cell.
Syntaxin-6 has been implicated in various pathological conditions, particularly in the context of cancer. Overexpression of STX6 has been observed in several types of human malignant tumors, including esophageal, colorectal, and renal cell carcinomas . Recent studies have highlighted its role in hepatocellular carcinoma (HCC), where it promotes tumor progression by enhancing the activation of the JAK-STAT signaling pathway . This makes Syntaxin-6 a potential therapeutic target for cancer treatment.
Recombinant human Syntaxin-6 is produced using conventional chromatography techniques and is typically expressed in E. coli . The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification and detection. It is used extensively in research to study the protein’s function, interactions, and role in disease mechanisms .
Recombinant human Syntaxin-6 is utilized in various experimental applications, including: