Analytical Data
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Gene name
DNM1L
- Application
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Alternative Names
Dnm1p/Vps1p-like protein (DVLP) (Dynamin family member proline-rich carboxyl-terminal domain less ) (Dymple) (Dynamin-like protein) (Dynamin-like protein 4) (Dynamin-like protein IV) (HdynIV) (Dynamin-related protein 1) (DLP1) (DRP1)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00429
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Expression Region
1-710aa
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Molecular Weight
84.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
DNM1L, also known as dynamin-like protein 1 (DLP1), is a member of the dynamin superfamily of GTPases, which are essential for membrane fission processes in eukaryotic cells. Research into DNM1L has gained significant attention due to its crucial role in mitochondrial dynamics, particularly in the regulation of mitochondrial fission. Abnormalities in DNM1L function have been associated with various neurodegenerative diseases, metabolic disorders, and mitochondrial dysfunctions, highlighting its importance in maintaining cellular health. Studies have shown that DNM1L exerts its effects by oligomerizing and wrapping around membranes, facilitating the constriction and eventual fission of mitochondria. The structural and functional analysis of DNM1L recombinant protein has provided insights into its mechanism of action and the regulation of its activity, which is influenced by GTP binding and hydrolysis. Moreover, understanding the biochemical characteristics of DNM1L through recombinant protein studies allows for the exploration of potential therapeutic targets for diseases linked to mitochondrial dysfunction. Advances in recombinant DNA technology have made it possible to produce DNM1L in a heterologous system, enabling detailed investigations of its function and interactions with other proteins. This research is vital for developing strategies to manipulate DNM1L activity in a therapeutic context, potentially alleviating conditions resulting from mitochondrial dysregulation. Overall, the study of DNM1L recombinant protein represents a promising area of investigation within cell biology and medicine, as it bridges the gap between basic research and clinical applications.
