Analytical Data
-
Gene name
FNBP1
- Application
-
Alternative Names
FBP17
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96RU3
-
Expression Region
Ala348~Glu529
-
Molecular Weight
24.5kDa
-
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
FNBP1, or Fast Neural Breast Cancer Protein 1, is a multifunctional protein implicated in various cellular processes, including actin dynamics, endocytosis, and signal transduction. Its role as a crucial regulatory component in cellular morphology and motility makes it a significant focus in cancer research, particularly in understanding breast cancer metastasis. The interest in FNBP1 stems from its association with the progression of tumorigenesis and its potential as a therapeutic target. Studies have shown that FNBP1 influences cellular pathways that promote invasive behavior in cancer cells, highlighting its relevance in the dynamics of cancer biology. Given its involvement in key signaling pathways, researchers are now focused on the structural characterization of FNBP1 through recombinant protein techniques. This approach allows for the analysis of its functional domains and interactions with other cellular proteins, paving the way for the development of novel therapeutic strategies aimed at inhibiting its pro-tumorigenic activities. The advancement in recombinant protein technologies facilitates the production of FNBP1 in sufficient quantities for detailed functional studies, which could lead to a better understanding of its role in cancer and other diseases.
