Analytical Data
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Gene name
FANK1
- Application
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Alternative Names
1700007B22Rik; AI850911; Fank1; FANK1_HUMAN; Fibronectin type 3 and ankyrin repeat domains 1; Fibronectin type 3 and ankyrin repeat domains protein 1; Fibronectin type III and ankyrin repeat domains 1; HSD13
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TC84
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Expression Region
1-345aa
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Molecular Weight
54.3 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
FANK1, or Focal Adhesion Kinase 1, is a critical protein involved in various cellular processes, including cell adhesion, migration, and signal transduction. Its role in cancer biology has garnered considerable attention, given its influence on tumor progression and metastasis. Research has shown that FANK1 is overexpressed in several cancers, making it a potential biomarker and therapeutic target. Scientists are investigating recombinant FANK1 proteins to better understand its functional roles and interactions within cellular pathways. The generation of these recombinant proteins facilitates the study of FANK1's structure-function relationships, enabling the identification of key domains critical for its activity. By using various expression systems, researchers can produce large quantities of purified FANK1, allowing for detailed biochemical and biophysical analyses. This research aims to elucidate the molecular mechanisms underlying FANK1's involvement in cancer and to explore its potential as a target for therapeutic intervention. The characterization of recombinant FANK1 could pave the way for novel strategies in cancer treatment, aiming to inhibit its activity or disrupt its interactions with other cellular partners. Overall, the study of FANK1 recombinant proteins represents a significant step forward in understanding the complexities of cancer biology and could hold promise for future clinical applications.
