VTA1 Human

The recombinant human VTA1 protein is a single, non-glycosylated polypeptide chain consisting of 331 amino acids, with a molecular mass of approximately 36.5 kDa . It is often fused to a His-tag at the N-terminus to facilitate purification through chromatographic techniques . The protein solution typically contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol, and 200mM NaCl .

VTA1 is involved in the ESCRT pathway, which is critical for the sorting of ubiquitinated membrane proteins into multivesicular bodies (MVBs). This pathway is essential for the degradation of membrane proteins in lysosomes, a process vital for maintaining cellular homeostasis and regulating various signaling pathways. VTA1 specifically interacts with other ESCRT components to facilitate the formation and release of intraluminal vesicles within MVBs.

Recombinant VTA1 is widely used in biochemical and cellular research to study the mechanisms of the ESCRT pathway and its role in various cellular processes. It is also utilized in structural biology studies to understand the protein-protein interactions within the ESCRT machinery. Additionally, VTA1 has potential implications in understanding diseases related to dysfunctional protein sorting and degradation, such as neurodegenerative disorders and certain types of cancer.

The production of recombinant VTA1 involves cloning the VTA1 gene into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the protein is expressed and subsequently purified using affinity chromatography techniques, leveraging the His-tag for efficient isolation .