Recombinant Human KIF5A Protein, N-His

Introduction

Recombinant Human KIF5A Protein, also known as Kinesin Family Member 5A, is a motor protein that plays a crucial role in intracellular transport and cellular division. This protein is encoded by the KIF5A gene and is a member of the kinesin superfamily of proteins. Recombinant Human KIF5A Protein is widely used in various scientific and medical applications due to its unique structure and activity.

Structure of Recombinant Human KIF5A Protein

Recombinant Human KIF5A Protein is a large protein with a molecular weight of approximately 120 kDa. It consists of 963 amino acids and is composed of three major domains: a globular N-terminal motor domain, a central coiled-coil domain, and a globular C-terminal domain. The motor domain contains the ATP-binding site and is responsible for the movement of the protein along microtubules. The coiled-coil domain is involved in protein-protein interactions, while the C-terminal domain helps in cargo binding and regulation of motor activity.

The crystal structure of Recombinant Human KIF5A Protein has been determined, revealing the intricate details of its three-dimensional organization. The motor domain is highly conserved among all kinesin family members and shows a characteristic fold with a central beta-sheet surrounded by alpha-helices. The coiled-coil domain forms a long helical structure, which is essential for the dimerization of the protein. The C-terminal domain is unique to KIF5A and contains a globular fold with a beta-sheet and several alpha-helices.

Activity of Recombinant Human KIF5A Protein

Recombinant Human KIF5A Protein is a molecular motor that utilizes the energy from ATP hydrolysis to move along microtubules. It is a plus-end directed motor, meaning it moves towards the plus end of the microtubule. This protein has been shown to be involved in the transport of various cargoes, including organelles, vesicles, and proteins, within the cell. It is also essential for the formation and maintenance of the mitotic spindle during cell division.

The activity of Recombinant Human KIF5A Protein is regulated by several factors, including post-translational modifications, protein-protein interactions, and binding to cargo. Phosphorylation of specific residues in the motor domain has been shown to modulate the motor activity of KIF5A. Additionally, interactions with other proteins, such as dynactin and kinesin light chain, can also affect the movement of this protein. The cargo binding site in the C-terminal domain allows for the specific transport of different cargoes by Recombinant Human KIF5A Protein.

Applications of Recombinant Human KIF5A Protein

Recombinant Human KIF5A Protein has a wide range of applications in the fields of cell biology, neuroscience, and medicine. Its role in intracellular transport makes it an essential tool for studying the mechanisms of cellular trafficking and division. This protein has been used in in vitro assays to study the motility and processivity of kinesin motors and their interactions with microtubules and other proteins.

Recombinant Human KIF5A Protein has also been implicated in various neurological disorders, such as amyotrophic lateral sclerosis (ALS) and hereditary spastic paraplegia (HSP). Mutations in the KIF5A gene have been linked to these diseases, and studies have shown that these mutations affect the motor activity and cargo binding of Recombinant Human KIF5A Protein. Therefore, this protein can serve as a potential therapeutic target for these disorders.

In addition, Recombinant Human KIF5A Protein has been used in drug discovery and development as a target for small molecule inhibitors. These inhibitors can block the motor activity of KIF5A