Recombinant Human GFM1 Protein, N-His

Reference: YHK94901
Product nameRecombinant Human GFM1 Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight27.05 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 TypeArg526-Asn751
Aliases /SynonymsElongation factor G1, GFM, GFM1, EFG1, mEF-G 1, Elongation factor G, mitochondrial, EF-Gmt, EFG, hEFG1, Elongation factor G 1, mitochondrial
ReferenceYHK94901
NoteFor research use only.

Description of Recombinant Human GFM1 Protein, N-His

Introduction

Recombinant Human GFM1 Protein is a highly purified protein that is produced through recombinant DNA technology. This protein plays a crucial role in the cell by aiding in the process of protein synthesis. GFM1 stands for “G elongation factor mitochondrial 1” and is found in the mitochondria of eukaryotic cells. In this article, we will discuss the structure, activity, and applications of this important protein.

Structure of Recombinant Human GFM1 Protein

Recombinant Human GFM1 Protein is a 68 kDa protein that consists of 624 amino acids. It is composed of three domains: the N-terminal domain, the central domain, and the C-terminal domain. The N-terminal domain contains a GTP-binding site, which is essential for the activity of the protein. The central domain is responsible for the interaction with other proteins, while the C-terminal domain is involved in the binding of the protein to the ribosome.

The crystal structure of Recombinant Human GFM1 Protein has been determined, revealing the exact arrangement of the three domains. It has been found that the protein exists as a homodimer, with each monomer containing all three domains. The dimerization of the protein is crucial for its activity, as it allows for the proper interaction with other proteins and the ribosome.

Activity of Recombinant Human GFM1 Protein

The main function of Recombinant Human GFM1 Protein is to act as a translation elongation factor in the process of protein synthesis. It binds to the ribosome and helps in the incorporation of amino acids into the growing polypeptide chain. This process is essential for the production of functional proteins in the cell.

In addition to its role in translation, Recombinant Human GFM1 Protein has also been found to play a role in mitochondrial protein import. It interacts with other proteins involved in this process and helps in the proper targeting of proteins to the mitochondria.

Applications of Recombinant Human GFM1 Protein

Recombinant Human GFM1 Protein has several potential applications in research and medicine. One of the main applications is in the study of translation and protein synthesis. The availability of a highly pure and active form of this protein allows researchers to study its function and interactions with other proteins in detail.

Another potential application of Recombinant Human GFM1 Protein is in the development of novel antibiotics. As this protein is essential for protein synthesis, targeting it could potentially disrupt bacterial growth and lead to the development of new antibiotics.

In the field of medicine, Recombinant Human GFM1 Protein could have therapeutic applications in the treatment of diseases caused by mitochondrial dysfunction. Mitochondrial diseases are a group of disorders that are caused by defects in the mitochondria, and GFM1 has been found to play a crucial role in these disorders. By providing a recombinant form of this protein, it could potentially be used as a treatment for these diseases.

Conclusion

Recombinant Human GFM1 Protein is a highly important protein that plays a crucial role in translation and mitochondrial function. Its structure and activity have been extensively studied, and its potential applications in research and medicine are promising. With the availability of a pure and active form of this protein, it is expected to continue to be a valuable tool in understanding cellular processes and developing new treatments for diseases.

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