Analytical Data
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Gene name
DSTN
- Application
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Alternative Names
ADF; ACTDP; Actin Depolymerizing Factor; Actin Binding Protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60981
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Expression Region
Met1~Val165
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Molecular Weight
49kDa
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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
DSTN (Destrin), also known as gelsolin-related protein, is a member of the actin-binding protein family that plays a crucial role in the dynamic regulation of the actin cytoskeleton. The actin cytoskeleton is essential for various cellular processes such as motility, shape maintenance, and division. Abnormal regulation of actin dynamics is linked to several diseases, including cancer and neurodegenerative disorders. Research on DSTN has gained attention due to its potential involvement in these pathological conditions, particularly in how it interacts with actin filaments to influence cell behavior. Recent studies have focused on the characterization of DSTN's structure, functional mechanisms, and its regulatory role in cellular processes. Understanding the reorganization of DSTN in cellular contexts can provide insights into therapeutic targets for conditions where actin dynamics are disrupted. This research aims to elucidate the molecular pathways involving DSTN and its interactions with other proteins, offering the possibility of developing interventions that can modulate its activity to restore normal cellular function and mitigate disease progression.
