Analytical Data
-
Gene name
SVIL
- Application
-
Alternative Names
SVIL；Supervillin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O95425
-
Expression Region
全长
-
AA Sequence
full
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SVIL (Svilin), a member of the giant protein family, plays a critical role in various cellular processes, particularly in muscle development and cell adhesion. Research into SVIL was primarily driven by its significant implications in myogenesis and the maintenance of skeletal muscle integrity. Abnormalities in SVIL expression have been associated with muscular dystrophies and other myopathies, making it a target for understanding muscular disorders. As a fibrous protein, SVIL is thought to contribute to the structural organization of the cytoskeleton, linking cells to extracellular matrices and facilitating mechanical stability. Advances in proteomics and molecular biology techniques have enabled the study of SVIL at the structural and functional levels, revealing insights into its interactions with other proteins and its regulatory mechanisms. Additionally, the potential of SVIL as a biomarker for muscle-related diseases has sparked interest in therapeutic applications aimed at modulating its expression or function. The ongoing exploration of SVIL's role in cellular mechanisms continues to provide a foundation for innovative strategies in muscle regeneration and repair, emphasizing its importance in both basic and translational research in muscle biology.
