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We validate the specificity of these antibodies to Dynamin-1-like protein by testing them on tissues known to express DNM1L positively and negatively. Browse below to find the DNM1L antibody that suites your experiment. We have 9 of these antibodies and many publications and validation images.
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Facts about Dynamin-1-like protein.
The specific recruiting at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:29899447). While the recruitment from the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation in the receptors and allows DNM1L filaments to float into closed rings that are probably enough to sever a double membrane (PubMed:29899447).
|TRAFAC class dynamin-like GTPase superfamily|
DLP1; DRP1Dnm1p/Vps1p-like protein; DVLPEC 22.214.171.124; Dymple; DYMPLEDYNIV-11; dynamin 1-like; Dynamin family member proline-rich carboxyl-terminal domain less; dynamin-1-like protein; Dynamin-like protein 4; Dynamin-like protein IV; Dynamin-like protein; Dynamin-related protein 1; FLJ41912; HDYNIV; VPS1
|Sequence:||12; NC_000012.12 (32679200..32745650)|
Ubiquitously expressed with highest levels found in skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. Isoform 2 and isoform 3 are predominantly expressed in testis and skeletal muscles respectively. Isoform 4 is weakly expressed in brain, heart and kidney. Isoform 5 is dominantly expressed in liver, heart and kidney. Isoform 6 is expressed in neurons.
Cytoplasm, cytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome. Membrane, clathrin-coated pit. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Colocalized with MARCHF5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Ass
When using the DNM1L Marker to measure the amount of DNM1 in a cell, you must use the correct conditions to achieve the desired results. To do this, you must use a Boster Bio optimization guide. This guide provides useful tips and tricks that will help you to optimize your experiments and improve your results. In the process of using the Boster Bio, you will surely experience some troubleshooting issues. Troubleshooting guides can help you identify these problems and how to fix them.
The DNM1L marker plays a role in the division of mitochondria and peroxisomes. In this process, the protein forms tubular structures associated with the membranes. These filaments wrap around the scission site and sever the mitochondrial membrane. These filaments are mediated by membrane receptors. When the filaments curl into closed rings, they are sufficient to sever the double membrane.
DNM1L is a homotetramer that dimersizes through its N-terminal GTP middle region and GED domain. The protein dimersizes through this mechanism and interacts with many proteins, including BCL2L1, FIS1, and PPP3CA. It regulates the transition of mitochondria. It also interacts with BCL2L1 and FIS1, and regulates GTP hydrolysis.
Clinical studies of mitochondrial diseases are characterized by their morphological heterogeneity, and are a consequence of mutations in nuclear and mitochondrial genes. Whole-exome sequencing has uncovered nuclear genes involved in mitochondrial dynamics. DNM1L encodes a protein called dynamin-related protein 1 (DRP1), which is an important component of the fission machinery in mitochondria. Dysfunction of Drp1 impairs neuronal function, particularly in neurons. Mutated mice display hypoplasia and smaller forebrains.
The DNM1L marker is a homotetramer that dimerizes through the N-terminal GTP middle region and the GED domain. The DNM1L molecule is also capable of self-assembly into multimeric ring-like structures. It interacts with several other proteins, including BCL2L1, FIS1, and UBE2I. It is also known to regulate the transition to mitochondria.
This protein is highly conserved between mice and humans. The protein DNM1L displays 98% homology between human and mouse proteins. Furthermore, it shares 96% of its M domain with zebrafish. Thus, the DNM1L marker can be used to determine whether a patient has this disease. Therefore, validation of the DNM1L marker is highly recommended. Its validation will provide a reliable and accurate gene-expression profile for DNM1L-related diseases.
There is a strong possibility that DNM1L may be involved in the genetics of MEFS. Its p.Arg403Cys mutation might identify patients who share similar presentations and a deficiency in mitochondrial fission. This would ultimately lead to a defective immune response and synaptic dysfunction. Despite the difficulties associated with this mutation, the new DNM1L marker has many potential applications.
The DNM1L gene encodes a protein known as dynamin-related-like-protein-1. The protein forms a multimeric collar at specific fission sites. When functionally altered, DNM1L is required for the efficient functioning of the mitochondrial fission machinery. Mutations of the DNM1L gene have a profound impact on the function of DNM1L.
A great guide for optimizing ELISA experiments is available from Boster. Listed below are tips to help optimize your experiments. Boster's gene infographics provide basic information about the different genes found in human and mouse cells. Boster also offers a gene search bar that allows you to find any gene that interests you. If you're unsure about a particular marker or the ELISA protocol, these guides and tips will help you out.
The DNM1L gene encodes a protein called DRP1 which regulates the activity of mitochondria and thereby regulates pro-fission. Biallelic nonsense mutations in this gene have been associated with severe encephalopathy and peripheral neuropathy. It also encodes two proteins called MID51 and MID49. The DNM1L gene is a homotetramer and dimerizes via its N-terminal GTP-binding domain. It is also a member of the Dynamin/Fzo/YdjA family.
*More publications can be found for each product on its corresponding product page