Recombinant Human DRP1/DNM1L, N-His

Reference: YHA11501
Product nameRecombinant Human DRP1/DNM1L, N-His
Uniprot IDO00429
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
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)
Aliases /SynonymsDynamin family member proline-rich carboxyl-terminal domain less, DVLP, Dynamin-like protein IV, Dynamin-related protein 1, Dynamin-like protein, DLP1, Dymple, Dynamin-1-like protein, HdynIV, Dnm1p/Vps1p-like protein, DRP1, DNM1L, Dynamin-like protein 4
ReferenceYHA11501
NoteFor research use only

Description of Recombinant Human DRP1/DNM1L, N-His

Introduction:

Recombinant Human DRP1/DNM1L, N-His is a protein that plays a crucial role in mitochondrial fission, a process that is essential for maintaining the health and function of mitochondria. This protein has been identified as a potential drug target for various diseases, making it a subject of intense research in the field of medicine.

Structure:

DRP1/DNM1L, N-His is a 736 amino acid protein that belongs to the dynamin family of GTPases. It is composed of five distinct domains – GTPase, middle, insert B, stalk, and GED – each of which has a specific function in regulating the protein’s activity. The GTPase domain is responsible for binding and hydrolyzing GTP, which is essential for the protein’s function. The middle domain acts as a spacer between the GTPase and insert B domains, while the insert B domain is involved in membrane binding. The stalk domain is responsible for oligomerization of the protein, and the GED domain regulates the protein’s GTPase activity.

Activity:

The main function of DRP1/DNM1L, N-His is to facilitate mitochondrial fission, a process that involves the division of mitochondria into smaller units. This process is essential for maintaining the proper functioning of mitochondria, as it allows for the distribution of mitochondria throughout the cell and the removal of damaged or dysfunctional mitochondria. DRP1/DNM1L, N-His plays a crucial role in this process by forming a spiral-like structure around the mitochondria and constricting it, leading to its division into two separate mitochondria.

In addition to its role in mitochondrial fission, DRP1/DNM1L, N-His has also been found to play a role in apoptosis, a process of programmed cell death. It is involved in the release of cytochrome c from mitochondria, which triggers the cascade of events leading to apoptosis. This makes DRP1/DNM1L, N-His an important protein in maintaining cellular homeostasis and preventing the development of diseases such as cancer.

Application:

The potential of DRP1/DNM1L, N-His as a drug target has been recognized in various diseases, including neurodegenerative disorders, cardiovascular diseases, and cancer. In neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease, mitochondrial dysfunction has been implicated as a contributing factor. As DRP1/DNM1L, N-His plays a crucial role in maintaining mitochondrial health, targeting this protein could potentially help in the treatment of these diseases.

In cardiovascular diseases, mitochondrial dysfunction has also been linked to the development of heart failure. DRP1/DNM1L, N-His has been identified as a potential target for preventing or treating heart failure by regulating mitochondrial fission and maintaining mitochondrial function.

In cancer, DRP1/DNM1L, N-His has been found to be dysregulated in various types of cancer, including breast, lung, and colon cancer. Targeting this protein could potentially inhibit cancer cell growth and proliferation, making it a promising target for cancer treatment.

Conclusion:

In conclusion, Recombinant Human DRP1/DNM1L, N-His is a crucial protein involved in mitochondrial fission and apoptosis, making it an important drug target for various diseases. Its structure and activity have been extensively studied, and its potential applications in the treatment of neurodegenerative disorders, cardiovascular diseases, and cancer make it a subject of ongoing research and development in the field of medicine.

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