Recombinant Human VTI1A Protein, N-His from ProteoGenix; catalogue ARO-P11597; research use only.
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Recombinant Human VTI1A Protein is a type of recombinant protein that plays a crucial role in various cellular processes. It is a membrane protein that belongs to the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family and is involved in vesicle trafficking and fusion. This protein is encoded by the VTI1A gene and is expressed in various tissues, including the brain, heart, and skeletal muscle.
The recombinant form of VTI1A protein is a 23 kDa protein with a molecular weight of 204 amino acids. It contains a single transmembrane domain and is composed of three domains: the N-terminal domain, the central coiled-coil domain, and the C-terminal domain. The N-terminal domain is responsible for binding to other SNARE proteins, while the central coiled-coil domain is involved in protein-protein interactions. The C-terminal domain is responsible for membrane anchoring and fusion activity.
Recombinant Human VTI1A Protein also contains a conserved SNARE motif, which is essential for its function in vesicle fusion. This motif is composed of a glutamine residue followed by a hydrophobic amino acid and a leucine residue. The SNARE motif is responsible for the specific interaction between VTI1A and other SNARE proteins, leading to the formation of a stable SNARE complex.
The main function of Recombinant Human VTI1A Protein is to regulate vesicle trafficking and fusion in various cellular processes. It is involved in the transport of vesicles from the endoplasmic reticulum (ER) to the Golgi apparatus, as well as from the trans-Golgi network to the plasma membrane. This protein is also essential for the fusion of vesicles with the lysosomes, which is crucial for the degradation of cellular waste and recycling of cellular components.
Recombinant Human VTI1A Protein interacts with other SNARE proteins, such as SNAP25 and Syntaxin, to form a SNARE complex. This complex is responsible for bringing the vesicle and target membrane close together, facilitating the fusion of the two membranes. This fusion process is essential for the delivery of cargo molecules, such as proteins and lipids, to their specific destinations within the cell.
In addition to its role in vesicle fusion, Recombinant Human VTI1A Protein has also been implicated in other cellular processes, such as autophagy and cytokinesis. Autophagy is a process in which damaged or unnecessary cellular components are degraded, while cytokinesis is the final stage of cell division. Both of these processes require the proper functioning of vesicle trafficking and fusion, which is regulated by VTI1A.
Recombinant Human VTI1A Protein has a wide range of applications in both research and medical fields. Its role in vesicle trafficking and fusion makes it a crucial protein for studying various cellular processes. It can be used to investigate the mechanisms underlying autophagy, cytokinesis, and other cellular processes that involve vesicle fusion. This protein can also be used to study the interactions between SNARE proteins and their role in membrane fusion.
In the medical field, Recombinant Human VTI1A Protein has potential applications in the treatment of diseases associated with defects in vesicle trafficking and fusion. For example, mutations in the VTI1A gene have been linked to a rare genetic disorder called Hermansky-Pudlak syndrome, which is characterized by abnormal vesicle trafficking in various tissues. Recombinant VTI1A protein can be used to study the underlying mechanisms of this disorder and potentially develop targeted therapies.
ProteoGenix catalogue number ARO-P11597. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 24.59 kDa; Fragment: Met1-Arg192; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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