Analytical Data
-
Gene name
FLNC
- Application
-
Alternative Names
FLNC；ABPL；FLN2；Filamin-C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14315
-
Expression Region
1-265aa
-
AA Sequence
MMNNSGYSDAGLGLGDETDEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPG
-
Molecular Weight
37.3 kDa
-
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
The study of FLNC (filamin C) recombinant protein is situated within the broader context of cellular mechanics and muscle development. FLNC is a member of the filamin family of actin-binding proteins, which play critical roles in organizing the cytoskeleton and maintaining cellular structure. Mutations in the FLNC gene have been associated with various genetic disorders, including familial cardiomyopathies and skeletal muscle diseases. Understanding the structure and function of FLNC is crucial for elucidating the mechanisms underlying these pathologies. Recent advances in recombinant protein technology have facilitated the production and analysis of FLNC, enabling researchers to investigate its biophysical properties, interactions with other cellular components, and its impact on cell motility and signaling pathways. This research not only aims to clarify FLNC's role in muscle function and integrity but also seeks to identify potential therapeutic targets for conditions arising from FLNC dysfunction. Through the detailed examination of recombinant FLNC, scientists hope to uncover insights that could lead to innovative treatments for muscle-related diseases, highlighting the importance of this protein in both fundamental biology and clinical applications.
