Analytical Data
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Gene name
DYSF
- Application
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Alternative Names
FER1L1; LGMD2B; Dysferlin,Limb Girdle Muscular Dystrophy 2B(Autosomal Recessive); Fer-1-like protein 1; Dystrophy-associated fer-1-like protein
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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 90% as determined by SDS-PAGE.
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Uniprot
O75923
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Expression Region
Met1~Tyr479
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Molecular Weight
57kDa
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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
The research on DYSF recombinant proteins is rooted in the understanding of dysferlin (DYSF), a vital protein that plays a crucial role in muscle membrane repair and maintenance. Mutations in the DYSF gene are linked to a group of genetic disorders collectively known as dysferlinopathies, including Limb-Girdle Muscular Dystrophy Type 2B and Miyoshi Myopathy, which lead to progressive muscle degeneration and weakness. Given the absence of effective treatments for these debilitating conditions, scientists have focused on producing recombinant DYSF proteins to investigate their structural and functional properties. By generating these recombinant proteins in laboratory settings, researchers aim to better understand the mechanisms of muscle repair and the consequences of DYSF mutations. This research not only enhances our knowledge of muscle biology but also explores potential therapeutic strategies, such as gene therapy or protein replacement, to restore functional dysferlin levels in affected individuals. The study of DYSF recombinant proteins is thus pivotal in uncovering new insights into muscle pathophysiology and developing future treatment modalities for dysferlinopathies.
