Recombinant Human SNAP29 Protein, N-His-SUMO & C-Strep

Description of Recombinant Human SNAP29 Protein, N-His-SUMO & C-Strep

Introduction

Recombinant Human SNAP29 Protein, also known as synaptosomal-associated protein 29, is a key protein involved in the process of membrane fusion. This protein plays a crucial role in the formation of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex, which is responsible for the fusion of vesicles with the target membrane in various cellular processes. In this article, we will explore the structure, activity, and application of Recombinant Human SNAP29 Protein.

Structure of Recombinant Human SNAP29 Protein

Recombinant Human SNAP29 Protein is a 295 amino acid protein with a molecular weight of 33 kDa. It belongs to the SNAP family of proteins, which are characterized by the presence of a central coiled-coil domain and an N-terminal domain. The coiled-coil domain of SNAP29 is responsible for its interaction with other proteins, while the N-terminal domain is involved in the binding of SNAP29 to the SNARE complex.

The crystal structure of Recombinant Human SNAP29 Protein has been determined, revealing a four-helix bundle structure with a conserved hydrophobic core. This structure is essential for the protein’s stability and function in membrane fusion.

Activity of Recombinant Human SNAP29 Protein

Recombinant Human SNAP29 Protein is primarily known for its role in membrane fusion. It is involved in the fusion of vesicles with the target membrane in various cellular processes, such as exocytosis, endocytosis, and intracellular membrane trafficking. This process is crucial for the proper functioning of cells, as it allows for the transport of molecules and organelles within the cell and communication between cells.

SNAP29 functions by binding to the SNARE complex, which is formed by the interaction of three other proteins: syntaxin, SNAP25, and VAMP (vesicle-associated membrane protein). This interaction leads to the formation of a stable complex that brings the vesicle and the target membrane in close proximity, allowing for the fusion of the two membranes.

In addition to its role in membrane fusion, Recombinant Human SNAP29 Protein has also been shown to play a role in autophagy, a process of cellular self-degradation. It interacts with the autophagy-related protein ATG14 to regulate the formation of autophagosomes, which are responsible for the degradation of unwanted or damaged cellular components.

Application of Recombinant Human SNAP29 Protein

Recombinant Human SNAP29 Protein has a wide range of applications in both research and therapeutic fields. Its role in membrane fusion makes it a valuable tool for studying cellular processes such as exocytosis and endocytosis. It can also be used to investigate the mechanisms of diseases that are caused by defects in membrane fusion, such as neurodegenerative disorders and lysosomal storage diseases.

In the therapeutic field, Recombinant Human SNAP29 Protein has shown potential in the treatment of diseases related to autophagy dysregulation. It has been found to play a role in the formation of autophagosomes, making it a potential target for the development of drugs to treat autophagy-related diseases.

Furthermore, Recombinant Human SNAP29 Protein has been used in the development of diagnostic tools for various diseases. It has been identified as an antigen in autoimmune diseases, such as systemic lupus erythematosus and rheumatoid arthritis, and can be used in the detection of autoantibodies in patient samples.

Conclusion

In conclusion, Recombinant Human SNAP29 Protein is a crucial protein involved in the process of membrane fusion. Its structure, activity, and diverse applications make it a valuable tool for research and therapeutic purposes. Further studies on this protein can provide a better understanding of its role in cellular processes and its potential as a target for the treatment of various diseases.