Analytical Data
-
Gene name
FILIP1
- Application
-
Alternative Names
FILIP1；KIAA1275；Filamin-A-interacting Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q7Z7B0
-
Expression Region
71-260aa
-
AA Sequence
KSLELSKEDLIQLLSIMEGELQAREDVIHMLKTEKTKPEVLEAHYGSAEPEKVLRVLHRDAILAQEKSIGEDVYEKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQ
-
Molecular Weight
30.2 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
FILIP1 (Filamin A Interacting Protein 1) is a relatively novel protein that has garnered attention in the field of cell biology due to its potential roles in cytoskeletal dynamics and cellular signaling. It is known to interact with filamin A, an important actin-binding protein that contributes to the organization of the cytoskeleton and cellular architecture. Previous studies have suggested that FILIP1 may play a critical role in regulating cell adhesion, migration, and mechanotransduction, processes that are essential for various physiological functions and developmental processes. Additionally, dysregulation of FILIP1 expression has been implicated in several diseases, including cancer, where it may influence tumor progression and metastasis. Researchers are keen to explore the functional mechanisms of FILIP1 as well as its interactions with filamin A and other cytoskeletal components. Understanding these pathways may uncover novel therapeutic targets for diseases characterized by cytoskeletal abnormalities and inform strategies to modulate cellular behaviors in both health and disease. As such, FILIP1 represents a promising avenue for further investigation in the realms of cell motility, tissue engineering, and potential clinical applications.
