Analytical Data
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Gene name
FILIP1L
- Application
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Alternative Names
FILIP1L；COL4A3BPIP；DOC1；GIP90；Filamin A-interacting Protein 1-like
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q4L180
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Expression Region
1-200aa
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AA Sequence
MVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQE
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Molecular Weight
55.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
FILIP1L (Filamin A-Interacting Protein 1-Like) is a relatively recently discovered protein that plays a significant role in cellular processes, particularly in the regulation of cytoskeletal dynamics and cell signaling. The study of FILIP1L is particularly important due to its involvement in various physiological and pathological conditions, including developmental processes, cancer progression, and neurodegenerative diseases. Research has indicated that FILIP1L interacts with filamin, a cytoskeletal protein that contributes to cellular structure and stability, thus highlighting its potential impact on cell morphology and motility. Moreover, emerging evidence suggests that alterations in FILIP1L expression or function may lead to significant dysregulation of cellular homeostasis and contribute to diseases. Therefore, understanding the molecular mechanisms underlying FILIP1L activity, as well as its interactions with other cellular components, could provide valuable insights into its biological functions and therapeutic potential. The recombinant production of FILIP1L offers a promising approach for detailed biochemical and biophysical studies, facilitating the exploration of its functional roles and the development of novel strategies for targeting related pathological conditions.
