Recombinant Human FTMT, N-His

Reference: YHJ22001
Product nameRecombinant Human FTMT, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight24.36 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 TypeLeu49-Asn242
Aliases /SynonymsFerritin, mitochondrial, FTMT
ReferenceYHJ22001
NoteFor research use only.

Description of Recombinant Human FTMT, N-His

Introduction

Recombinant Human FTMT (ferroportin mitochondrial) is a protein that plays a crucial role in iron metabolism and is encoded by the SLC40A1 gene. It is a transmembrane protein that is primarily located in the mitochondria, but it is also found in other tissues such as the liver, spleen, and heart. In this article, we will discuss the structure, activity, and application of Recombinant Human FTMT.

Structure of Recombinant Human FTMT

Recombinant Human FTMT is a 62 kDa protein that consists of 585 amino acids. It is a transmembrane protein with six transmembrane domains, a large extracellular loop, and a short cytoplasmic tail. The N-terminus of the protein is located in the cytoplasm, while the C-terminus is located in the mitochondrial matrix.

The structure of FTMT is highly conserved among different species, with over 90% similarity between human and mouse sequences. This highlights the importance of this protein in iron metabolism and its evolutionary significance.

Activity of Recombinant Human FTMT

FTMT is a ferroportin, which means it is responsible for transporting iron out of the cell. It is specifically involved in the transport of iron from the mitochondria to the cytoplasm. This process is essential for maintaining iron homeostasis in the cell.

FTMT works in conjunction with other proteins, such as ferroportin 1 (FPN1) and ferroportin 2 (FPN2), to regulate the levels of iron in the cell. It is also regulated by hepcidin, a hormone that controls iron absorption and distribution in the body.

Mutations in the SLC40A1 gene, which encodes FTMT, have been linked to various disorders, including hemochromatosis, a condition characterized by excessive iron accumulation in the body. This further emphasizes the critical role of FTMT in iron metabolism.

Application of Recombinant Human FTMT

Recombinant Human FTMT has various applications in both research and clinical settings. One of the main uses of this protein is in the study of iron metabolism and its related disorders. Researchers can use recombinant FTMT to investigate the function of this protein and its role in iron transport.

In the clinical setting, recombinant FTMT can be used as an antigen to develop diagnostic tests for iron-related disorders. It can also be used as a therapeutic target for the treatment of these disorders. For example, targeting FTMT with specific inhibitors may help regulate iron levels in patients with hemochromatosis.

Moreover, recombinant FTMT can also be used in the production of antibodies for research and diagnostic purposes. These antibodies can be used to detect the presence of FTMT in different tissues and to study its expression patterns.

Conclusion

Recombinant Human FTMT is a transmembrane protein that plays a crucial role in iron metabolism. It is involved in the transport of iron from the mitochondria to the cytoplasm and is regulated by various factors. Mutations in the gene encoding FTMT can lead to iron-related disorders, highlighting the importance of this protein in maintaining iron homeostasis.

Recombinant FTMT has various applications in research and clinical settings, including the study of iron metabolism and the development of diagnostic tests and therapeutic targets for iron-related disorders. Further research on this protein may lead to a better understanding of its function and potential therapeutic interventions.

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