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Dynamins (EC 220.127.116.11) are multi-domain, high molecular weight GTPases, which play a key role in receptor-mediated endocytosis, synaptic vesicle recycling, motility of cancer cells and spermatogenesis. Mutations in DNM2 have been linked to neuromuscular diseases.
|Cat. No.||Product Name / Activity|
|1774||Dynamin inhibitory peptide|
|1775||Dynamin inhibitory peptide, myristoylated|
|Cell-permeable dynamin inhibitor|
|1776||Dynamin inhibitory peptide, myristoylated (control)|
|Control peptide version of dynamin inhibitory peptide, myristoylated (Cat. No. 1775)|
|Non-competitive dynamin inhibitor|
|Dynamin I inhibitor|
|Dynamin inhibitor; analog of dynasore (Cat. No. 2897)|
|6799||MB 0223 New|
|Dynamin-related GTPase DRP1 partial inhibitor|
|Selective dynamin inhibitor; attenuates mitochondrial division and apoptosis|
|Dynamin-related protein 1 (Drp1) inhibitor; cell-permeable|
Dynamins (EC 18.104.22.168) are multi-domain, high molecular weight GTPases, which play a key role in receptor-mediated endocytosis, synaptic vesicle recycling, focal adhesion assembly, cytoskeletal changes, motility of cancer cells and spermatogenesis. The dynamin family also includes dynamin-like proteins.
In mammals, there are three classical dynamins, each coded by a different gene, with varying expression patterns. Dynamin I is predominantly expressed in neurons and mediates synaptic vesicle recycling. Dynamin II is ubiquitously expressed and is involved in receptor mediated endocytosis, including uptake of viral and bacterial pathogens. The highest levels of dynamin III are found in the lung, testes and post-synaptic neurons and has been implicated in post-synaptic AMPA receptor recycling.
Dynamin proteins have various domains associated with different functions: the N-terminal GTPase domain to binds and hydrolyzes GTP; pleckstrin homology (PH) domains, which bind acidic membrane phospholipids; and C-terminal proline rich (PR) domains that mediate protein-protein interactions. Dynamin-like proteins, which assist in recruiting classical dynamins to cleave vesicles from the cell membrane, lack PH and PR domains.
Dynamins are associated with a range of disorders including, but not limited to, Alzheimer's disease, cancer metastasis, epilepsy, Huntington's disease and Parkinson's disease. Mutations in the dynamin II gene have been linked to two neuromuscular diseases; Centronuclear myopathy, and intermediate and axonal forms of Charcot-Marie Tooth disease.
Tocris offers the following scientific literature for Dynamin to showcase our products. We invite you to request* or download your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
Our new product guide highlights over 215 new products added to the Tocris Bioscience range during the first half of 2019.
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|