Analytical Data
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Gene name
DST
- Application
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Alternative Names
BP240; BPA; BPAG1; CATX-15; DMH; MACF2; Dystonia musculorum protein; Bullous Pemphigoid Antigen 1; Hemidesmosomal plaque protein; 230 kDa bullous pemphigoid antigen
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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
Q03001
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Expression Region
Met1~Thr252
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Molecular Weight
28kDa
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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
DST (Dystrophia Myotonica Protein Kinase) is a critical protein associated with various cellular processes, particularly in relation to muscle function and neuromuscular diseases. Research surrounding DST protein has gained momentum due to its implications in myotonic dystrophy, a hereditary condition characterized by progressive muscle wasting and weakness. The complexity of DST’s role in cellular signaling and its interaction with other proteins has prompted scientists to delve deeper into its structure and function. Recent advancements in molecular biology techniques, such as CRISPR-Cas9 gene editing and high-resolution imaging, have enabled researchers to manipulate and visualize DST in vivo, shedding light on its biomechanical properties and cellular localization. Moreover, understanding the pathways in which DST is involved could reveal novel therapeutic targets for managing myotonic dystrophy and related disorders. Given the significant impact of such diseases on quality of life, the study of DST protein and its reorganization in various cellular contexts opens new frontiers for medical research and potential drug development. As a result, the investigation of DST's structure, interactions, and functional dynamics is essential for unraveling the underlying mechanisms of myotonic dystrophy and providing insights into possible interventions. By exploring the intricate biology of DST, researchers aim to contribute to the broader field of protein research and its applications in combating genetic disorders.
