RALB Human

RALB is a GTP-binding protein that shares more than 50% homology with the Ras proteins . The human recombinant version of RALB is typically produced in Escherichia coli (E. coli) and is fused with a 24 amino acid His tag at the N-terminus . This recombinant protein is a single, non-glycosylated polypeptide chain containing 227 amino acids, with a molecular mass of approximately 25.6 kDa .

RALB, along with its closely related homolog RALA, plays a crucial role in cellular signaling pathways. These proteins are involved in the regulation of vesicle trafficking, cell migration, and cell cycle progression. RALB has been implicated in the regulation of apoptosis and autophagy, processes that are essential for maintaining cellular homeostasis .

In the context of cancer, RALB is considered a proto-oncogene. Its overexpression or mutation can lead to uncontrolled cell proliferation and tumorigenesis. Studies have shown that RALB is involved in the survival and metastasis of cancer cells, making it a potential target for cancer therapy .

The recombinant human RALB protein is produced using proprietary chromatographic techniques to ensure high purity. The protein is typically formulated in a sterile filtered colorless solution containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.1M NaCl, and 1mM DTT . The purity of the recombinant protein is greater than 90% as determined by SDS-PAGE .

For optimal stability, the recombinant RALB protein should be stored at -20°C for long-term storage. If the entire vial is to be used within 2-4 weeks, it can be stored at 4°C. To prevent degradation, it is recommended to avoid multiple freeze-thaw cycles .

Due to its role in cellular signaling and cancer, recombinant RALB is widely used in cancer research. It is utilized to study the molecular mechanisms underlying cancer cell survival, proliferation, and metastasis. Additionally, it serves as a valuable tool for developing targeted therapies aimed at inhibiting RALB function in cancer cells .