Analytical Data
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Gene name
FHIT
- Application
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Alternative Names
FHIT;Bis(5'-adenosyl)-triphosphatase
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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
P49789
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Expression Region
1-147aa
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AA Sequence
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH HHHHH
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Molecular Weight
18 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
FHIT (Fragile Histidine Triad) protein is a tumor suppressor that has garnered significant interest in cancer research due to its role in maintaining genomic stability and its involvement in various cellular processes, including apoptosis and DNA repair. The FHIT gene, located at chromosome 3p14.2, is frequently found to be deleted or mutated in several types of human cancers, particularly those of the lung, bladder, and head and neck. This loss of FHIT expression is correlated with tumor progression and poor prognosis, highlighting its importance in carcinogenesis. Research has focused on understanding the biochemical pathways through which FHIT exerts its tumor suppressive effects, as well as on developing recombinant FHIT protein for therapeutic purposes. Recombinant FHIT has been investigated for its potential application in cancer therapy, particularly as a tool for restoring function in cancer cells that exhibit FHIT loss, thereby reactivating its tumor-suppressive actions. Studies aimed at elucidating the structural and functional properties of the recombinant protein have provided insights into its interactions with other biomolecules and its mechanisms of action. Consequently, the development of recombinant FHIT protein represents a promising avenue for cancer treatment strategies and adds to the growing body of research exploring the therapeutic potential of tumor suppressor proteins.
