Analytical Data
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Gene name
DYSF
- Application
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Alternative Names
DYSF;FER1L1;Dysferlin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75923
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Expression Region
全长
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AA Sequence
full
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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
Dysferlin (DYSF) is a crucial protein associated with muscle membrane repair, and mutations in the DYSF gene are implicated in a range of muscular dystrophies, particularly Miyoshi myopathy and limb-girdle muscular dystrophy 2B. Research into DYSF recombinant proteins has gained momentum due to their potential therapeutic applications in treating these genetic disorders. The investigation of DYSF's structure and function is essential to understand its role in the membrane repair process and to develop effective strategies for gene therapy or protein replacement. Previous studies have demonstrated that dysferlin interacts with various components of the muscle cell membrane, facilitating the repair of sarcolemmal injuries following muscle contraction and damage. However, the heterogeneity of mutations that affect DYSF function complicates the development of targeted therapies. Recombinant DYSF proteins provide a valuable tool for studying these mutations' effects on protein function and for screening potential small molecules or compounds that could enhance muscle repair mechanisms. Furthermore, advances in technologies such as CRISPR/Cas9 gene editing raise the possibility of correcting DYSF mutations in patient-derived cells, paving the way for personalized medicine approaches in the management of dysferlinopathies. As such, ongoing research focuses not only on understanding the molecular mechanisms of dysferlin but also on exploring its therapeutic potential through innovative applications of recombinant protein technology. This research holds promise for improving the quality of life for individuals affected by dystrophies associated with DYSF deficiency, offering hope for future treatment options that could restore muscle function and overall mobility.











