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Brand: ProteoGenix

Recombinant Human GTPBP4 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
42.87 kDa

$392.00

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Met1–Gly350
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Recombinant Human GTPBP4 Protein, N-His

Recombinant Human GTPBP4 Protein, N-His

Product name Recombinant Human GTPBP4 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 42.87 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°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)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Met1-Gly350
Aliases /Synonyms Chronic renal failure gene protein, NOG1, CRFG, Nucleolar GTP-binding protein 1, GTPBP4, GTP-binding protein NGB
Reference ARO-P12132
Note For research use only.
Molecular Constructor
Met1–Gly350

Introduction

Recombinant Human GTPBP4 Protein is a highly purified and biologically active protein that is produced through recombinant DNA technology. It is a member of the GTP-binding protein family and plays a crucial role in various cellular processes, including protein synthesis, cell proliferation, and cell survival. In this article, we will explore the structure, activity, and applications of this important protein.

Structure of Recombinant Human GTPBP4 Protein

Recombinant Human GTPBP4 Protein is a 45 kDa protein that consists of 409 amino acids. It is composed of three domains: a GTPase domain, a KH domain, and a C-terminal domain. The GTPase domain is responsible for binding GTP and hydrolyzing it to GDP, which is essential for the protein’s activity. The KH domain is involved in RNA binding, and the C-terminal domain is responsible for protein-protein interactions.

Activity of Recombinant Human GTPBP4 Protein

Recombinant Human GTPBP4 Protein is a GTPase, which means it can bind to and hydrolyze GTP. This activity is essential for the protein’s role in protein synthesis. GTPBP4 binds to the small ribosomal subunit and promotes the binding of the initiator tRNA to the start codon of mRNA, thus initiating protein synthesis. It also plays a role in the termination of protein synthesis by promoting the release of the completed protein from the ribosome.

Furthermore, Recombinant Human GTPBP4 Protein has been shown to be involved in cell proliferation and survival. It interacts with various proteins involved in cell signaling pathways, such as the PI3K/AKT and MAPK pathways, and regulates their activity. This suggests that GTPBP4 may play a role in cell growth and survival.

Applications of Recombinant Human GTPBP4 Protein

Recombinant Human GTPBP4 Protein has a wide range of applications in both basic research and clinical settings. Its role in protein synthesis makes it a valuable tool for studying translation and its regulation. It can also be used to investigate the role of GTP-binding proteins in various cellular processes.

In the clinical setting, Recombinant Human GTPBP4 Protein has been studied as a potential biomarker for certain types of cancer. It has been found to be overexpressed in breast and lung cancer cells, and its expression levels have been correlated with tumor aggressiveness and patient survival. This suggests that GTPBP4 may serve as a diagnostic and prognostic marker for these cancers.

Moreover, Recombinant Human GTPBP4 Protein has been investigated as a potential therapeutic target for cancer treatment. Inhibition of GTPBP4 has been shown to decrease cell proliferation and induce apoptosis in cancer cells, making it a promising target for anti-cancer drugs.

Conclusion

Recombinant Human GTPBP4 Protein is a crucial protein involved in protein synthesis, cell proliferation, and cell survival. Its structure, activity, and potential applications make it an important tool for both basic research and clinical studies. Further research on this protein may lead to a better understanding of its role in cellular processes and its potential as a biomarker and therapeutic target for cancer.

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