Analytical Data
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Gene name
FAT1
- Application
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Alternative Names
(Cadherin family member 7)(Cadherin-related tumor suppressor homolog)(Protein fat homolog)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14517
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Expression Region
4203-4588aa
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Molecular Weight
49.2 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
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Protein Description
FAT1, a member of the cadherin superfamily, is a large transmembrane protein that plays a crucial role in cell adhesion, signaling, and tissue morphology. Its significance has been underscored by studies demonstrating that FAT1 is implicated in various biological processes, including development, cell migration, and oncogenesis. Aberrant expression of FAT1 has been associated with several cancers, particularly in epithelial tissues, indicating its potential as a tumor suppressor and a marker for tumor progression. Research into FAT1 recombinant protein has gained momentum due to its promising role in understanding cancer biology and developmental processes. The ability to produce FAT1 in a recombinant form allows for detailed structural and functional studies, enabling researchers to elucidate its mechanistic pathways and interactions at the cellular level. Furthermore, the use of FAT1 recombinant proteins in therapeutic applications, such as targeted drug delivery or gene therapy, has emerged as a compelling area of investigation. As researchers continue to explore the multifaceted roles of FAT1 in health and disease, the development and characterization of FAT1 recombinant proteins stand to provide vital insights into its physiological functions and the development of novel therapeutic strategies.
