Analytical Data
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Gene name
FAK1
- Application
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Alternative Names
PTK2; FADK; FAK1; Pp125FAK; PPP1R71; Protein Tyrosine Kinase 2; Focal adhesion kinase-related nonkinase; Protein phosphatase 1 regulatory subunit 71
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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 95% as determined by SDS-PAGE.
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Uniprot
Q05397
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Expression Region
Gly798~Ala1041
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Molecular Weight
33kDa
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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
FAK1 (Focal Adhesion Kinase 1) is a non-receptor protein tyrosine kinase critically involved in cellular processes such as proliferation, survival, migration, and differentiation. Its role in mediating integrin signaling at focal adhesions links the extracellular matrix to the cytoskeleton, thereby influencing cellular responses to their environment. Dysregulation of FAK1 has been implicated in various diseases, including cancer, where its overexpression is often associated with increased tumor progression and metastasis. Consequently, FAK1 has emerged as a promising therapeutic target in oncology. Researchers have been focusing on the development of recombinant FAK1 proteins to better understand its structural and functional characteristics, allowing for insights into its regulatory mechanisms. Such studies aim to elucidate how FAK1 interacts with other proteins and pathways, providing a foundation for potential drug design. Moreover, structural analysis of FAK1 can unveil conformational changes upon ligand binding, which is essential for understanding its activation and subsequent signaling cascades. Overall, further investigation into the recombinant expression and functional characterization of FAK1 is essential for developing innovative strategies to mitigate diseases associated with its aberrant activity.
