Analytical Data
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Gene name
Dynamitin (DCTN2)
- Application
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Alternative Names
P50; DCTN50; RBP50; 50 kDa dynein-associated polypeptide; Dynactin complex 50 kDa subunit; p50 dynamitin
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q13561
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Expression Region
Ala2~Lys401
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Molecular Weight
50kDa
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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
Related Products
Protein Description
Dynamitin, encoded by the DCTN2 gene, is a critical component of the dynactin complex, which plays a crucial role in intracellular transport and mitosis. The dynactin complex is essential for the function of motor proteins, particularly dynein, facilitating the retrograde transport of vesicles along microtubules. Dysregulation or mutations in DCTN2 are associated with various neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia, making its study pertinent for understanding the underlying mechanisms of these conditions. The generation of recombinant Dynamitin protein allows researchers to explore its structural characteristics, functional interactions, and the impact of specific mutations. By employing techniques such as biochemical assays, microscopy, and protein interaction studies, scientists aim to uncover how alterations in Dynamitin influence cellular transport processes and contribute to disease pathology. This research not only enhances our understanding of cellular dynamics but also holds potential for developing targeted therapeutic strategies for related neurodegenerative disorders.
