Price Breakdown,VDAC1 (MGC111064, PORIN) protein expression summary

The VDAC1 peptide is emerging as a significant area of research in the development of novel therapeutic strategies, particularly in the fight against cancer and metabolic disorders. Voltage-dependent anion channel 1 (VDAC1), a crucial mitochondrial outer membrane protein, plays a pivotal role in regulating cellular energy metabolism, apoptosis, and the transport of vital molecules. Its involvement in these fundamental cellular processes makes it an attractive target for therapeutic intervention.

Research has demonstrated that VDAC1-based peptides possess remarkable properties, including the ability to selectively kill peripheral blood mononuclear cells and selectively affect cancerous, but not non-cancerous cells. This targeted action is a key advantage, minimizing damage to healthy tissues while effectively combating disease. Studies have shown that these peptides can induce cell death in a variety of cancer types. For instance, VDAC1-based peptides have been shown to eliminate cancer stem cells in tumors and induce cell death in cultured cancer stem cells. This direct attack on cancer stem cells is particularly promising, as these cells are often responsible for tumor recurrence and resistance to conventional therapies.

The mechanism behind the efficacy of VDAC1 peptide lies in its ability to disrupt cellular functions. By binding to VDAC1, these peptides can interfere with critical cellular processes. VDAC1 mediates the transport of adenine nucleotides, calcium, and other metabolites in and out of mitochondria, thereby playing an important role in energy homeostasis. Disruption of this transport can lead to metabolic dysregulation within cancer cells. Furthermore, VDAC1 functions in the release of apoptotic proteins located in the mitochondrial intermembrane space. VDAC1-based peptides can modulate this function, promoting programmed cell death in malignant cells. The mode of action of VDAC1-based peptides often results in attacks on hallmarks of cancer and reversal of oncogenic properties, including critical mitochondrial functions.

Beyond cancer, VDAC1 peptide research is also exploring its potential in other areas. For example, a VDAC1 N-terminal peptide has shown promise in enhancing the survival of motor neuron-like cells in models of neurodegenerative diseases. Another study highlighted a voltage-dependent anion channel 1 (VDAC1)-based peptide, R-Tf-D-LP4, which arrested steatosis and NASH progression, suggesting potential applications in metabolic disorders. The development of oral peptide therapeutics for diabetes treatment is a broader field, and understanding the role of mitochondrial proteins like VDAC1 could offer new avenues.

The VDAC1 protein expression summary indicates that VDAC1 (MGC111064, PORIN) is expressed in various contexts, and its elevated presence in numerous human cancer cell lines compared to normal cells underscores its significance as a therapeutic target. VDAC1 is a prime target for the fight against cancer due to this differential expression. The mitochondrial voltage-dependent anion channel-1 (VDAC1) protein plays a central role in regulating mitochondrial metabolism and energy production. It is described as a non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrial outer membrane and plasma membrane. The VDAC1 gene encodes this crucial protein.

Researchers are actively investigating different VDAC1 peptide constructs. For instance, specific VDAC1-based peptides have been designed to target oncogenic pathways. The VDAC1 N-terminal peptide has been a focus of study for its ability to modulate cellular processes. Furthermore, the commercial availability of Vdac1 Peptide and Vdac1 Protein for research applications, including blocking/neutralizing, control, ELISA, protein array, and Western blot, facilitates further scientific inquiry. These VDAC1 Peptides and VDAC1 Proteins are valuable tools for researchers studying metabolic research studies.

It is important to note that VDAC1 is more than just a channel; it is VDAC1 interacts with about 150 proteins to regulate the integration of mitochondrial functions with other cellular activities. It is described as VDAC1 is the most abundant pore-forming protein of the outer mitochondrial membrane. The VDAC1 protein can also be found on the plasma membrane, and this form may have an extended N-terminal signal peptide responsible for its cellular targeting. The exploration of VDAC1 as a pharmacological target in cancer and other diseases is an active and growing field, with ongoing research into various peptides, small molecules, and microRNAs that exploit VDAC1 for therapeutic benefit. The development of VDAC1-targeted NHK1 peptide to recover mitochondrial function is another example of this extensive research.

In summary, VDAC1 peptide research represents a promising frontier in therapeutic development. The ability of these peptides to target critical cellular processes, selectively eliminate cancerous cells, and modulate mitochondrial function offers significant potential for treating a range of diseases, most notably cancer. Continued research into the precise mechanisms of action and the development of safe and effective VDAC1-based therapies holds great promise for the future