Recombinant Human NCL Protein, N-His & N-SUMO

Description of Recombinant Human NCL Protein, N-His & N-SUMO

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, where the DNA sequence encoding for a particular protein is inserted into a host organism’s genome. This allows for the production of large quantities of a specific protein in a controlled and efficient manner. One such recombinant protein is the Recombinant Human NCL Protein, which has gained significant attention in the scientific community due to its unique structure, diverse activities, and potential applications in various fields.

Structure of Recombinant Human NCL Protein

The human nucleolin (NCL) protein is a multifunctional protein that is involved in various cellular processes such as gene expression, DNA replication, and RNA metabolism. It is composed of 707 amino acids and has a molecular weight of approximately 76 kDa. The recombinant form of NCL is produced in E. coli using a plasmid vector containing the DNA sequence encoding for the protein. The resulting protein has the same amino acid sequence and structure as the native NCL protein found in humans.

The NCL protein consists of four main structural domains: the N-terminal domain, central domain, C-terminal domain, and glycine-rich domain. The N-terminal domain is responsible for binding to various proteins and nucleic acids, while the central domain contains four RNA recognition motifs (RRMs) that are involved in RNA binding. The C-terminal domain is responsible for the nuclear localization of NCL, and the glycine-rich domain is involved in protein-protein interactions.

Activity of Recombinant Human NCL Protein

The NCL protein is known to have diverse activities, which are essential for its various functions in the cell. One of its main activities is its ability to bind to nucleic acids, including DNA and RNA. This binding is facilitated by the RRM domains in the central domain of NCL. Through its interactions with nucleic acids, NCL plays a crucial role in regulating gene expression and DNA replication.

In addition to its nucleic acid binding activity, NCL also has a role in ribosome biogenesis, where it binds to ribosomal RNA and helps in the assembly of ribosomes. It also has a role in the transport of ribosomal proteins to the nucleolus, where ribosomes are assembled. Furthermore, NCL has been shown to have a role in the formation of stress granules, which are cytoplasmic structures that form in response to cellular stress.

Applications of Recombinant Human NCL Protein

Due to its diverse activities and essential functions in the cell, recombinant human NCL protein has potential applications in various fields of research. One of its main applications is in cancer research, where NCL has been shown to be overexpressed in various types of cancer. As such, it has been proposed as a potential biomarker for cancer diagnosis and a target for cancer therapy.

Furthermore, NCL has been shown to have a role in viral infections, where it interacts with viral proteins and plays a role in viral replication. This makes it a potential target for antiviral therapies. Additionally, NCL has been implicated in neurodegenerative diseases, and its potential role in these diseases is currently being investigated.

In the biotechnology industry, recombinant NCL protein has been used as an antigen in various immunoassays, such as ELISA and Western blot, for the detection of NCL in biological samples. It has also been used in structural studies to understand the interactions of NCL with other proteins and nucleic acids.

Conclusion

In summary, recombinant human NCL protein is a versatile protein with a unique structure and diverse activities. Its potential applications in various fields make it a valuable tool for research and a potential target for therapeutic interventions. Further studies on the structure and function of N