Analytical Data
-
Gene name
FLNb
- Application
-
Alternative Names
FLNb；FLN1L；FLN3；TABP；Filamin-B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O75369
-
Expression Region
2503-2602aa
-
AA Sequence
SAIPKASSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGP TTPCEEVSMKHVGNQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP
-
Molecular Weight
278 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
FLNb, or fibulin-5, is an extracellular matrix protein that plays a crucial role in various biological processes, including tissue development, angiogenesis, and cellular signaling. Research on FLNb has gained momentum due to its significant involvement in the structural integrity of elastic fibers and its implications in various pathologies, such as arterial diseases, cancer, and connective tissue disorders. Studies have shown that FLNb contributes to the assembly and stabilization of elastin fibers, which are vital for the elasticity and resilience of connective tissues. Moreover, alterations in FLNb expression and function have been linked to the progression of certain diseases. As a result, characterizing FLNb through recombinant protein techniques has become essential for understanding its function at the molecular level. This research aims to investigate the structural properties, interactions, and biological roles of FLNb in both physiological and pathological contexts, thereby providing insights into its potential as a therapeutic target. Developing recombinant FLNb allows for the exploration of its mechanism of action and potential applications in regenerative medicine and tissue engineering, highlighting the significance of this protein in health and disease.
