Recombinant Human GTPBP4 Protein, N-His

Reference: YHK53401
Product nameRecombinant Human GTPBP4 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight42.87 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeMet1-Gly350
Aliases /SynonymsChronic renal failure gene protein, NOG1, CRFG, Nucleolar GTP-binding protein 1, GTPBP4, GTP-binding protein NGB
ReferenceYHK53401
NoteFor research use only.

Description of Recombinant Human GTPBP4 Protein, N-His

Introduction to Recombinant Human GTPBP4 Protein

Recombinant Human GTPBP4 Protein, also known as GTP-binding protein 4, is a member of the GTP-binding protein family. It is encoded by the GTPBP4 gene and is found in the cytoplasm of human cells. This protein plays a crucial role in regulating the activity of GTPases, which are enzymes involved in multiple cellular processes such as cell signaling, protein synthesis, and cell division.

Structure of Recombinant Human GTPBP4 Protein

The Recombinant Human GTPBP4 Protein is a 45-kDa protein consisting of 408 amino acids. It contains a conserved GTP-binding domain, which is essential for its function. The protein also has a C-terminal domain that is responsible for its interaction with other proteins. The crystal structure of the GTPBP4 protein has been determined, revealing its unique structure and providing insights into its function.

Activity of Recombinant Human GTPBP4 Protein

The main activity of Recombinant Human GTPBP4 Protein is its ability to bind to and hydrolyze GTP, a process that is essential for regulating the activity of GTPases. GTPBP4 is known to interact with several GTPases, including elongation factor G and translation initiation factor eIF5B. By interacting with these GTPases, GTPBP4 plays a crucial role in protein synthesis and cell growth.

Moreover, studies have shown that GTPBP4 is involved in the regulation of mitochondrial function. It has been found to interact with mitochondrial ribosomes and regulate their activity, thus playing a crucial role in mitochondrial protein synthesis. This protein has also been linked to the regulation of mitochondrial DNA replication and maintenance.

Application of Recombinant Human GTPBP4 Protein

Recombinant Human GTPBP4 Protein has various applications in both research and medical fields. Its role in regulating GTPases makes it a valuable tool for studying cellular processes such as cell signaling and protein synthesis. Furthermore, its involvement in mitochondrial function makes it a potential target for the development of therapeutic interventions for mitochondrial diseases.

One of the major applications of Recombinant Human GTPBP4 Protein is in the field of cancer research. GTPBP4 has been found to be overexpressed in several types of cancer, including breast cancer and colorectal cancer. This overexpression has been linked to tumor growth and progression, making GTPBP4 a potential therapeutic target for cancer treatment.

In addition, Recombinant Human GTPBP4 Protein has been used in the development of diagnostic tools for various diseases. For instance, it has been used as an antigen in immunoassays to detect the presence of GTPBP4 antibodies in patients with autoimmune diseases such as systemic lupus erythematosus. This protein has also been used in the development of diagnostic tests for mitochondrial diseases.

Conclusion

In conclusion, Recombinant Human GTPBP4 Protein is a crucial protein involved in the regulation of GTPases and mitochondrial function. Its unique structure and activity make it a valuable tool for studying cellular processes and potential target for therapeutic interventions. Its diverse applications in research and medical fields make it a promising protein for further studies and developments.

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