Analytical Data
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Gene name
FNTA
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简介
FNTA protein is a key subunit in the farnesyltransferase and geranylgeranyltransferase complexes, which can transfer farnesyl or geranylgeranyl moieties to proteins with Cys-aliphatic-aliphatic-X sequence cysteine residues in proteins. This enzymatic activity contributes to post-translational protein modifications. FNTA Protein, Human is the recombinant human-derived FNTA protein, expressed by E. coli , with tag free.
- Application
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49354
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Expression Region
M1-Q379
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Protein Length
Full Length
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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
FNTA (Farnesyltransferase) is a key enzyme involved in the post-translational modification of proteins through farnesylation, a process that attaches farnesyl groups to the cysteine residue of certain proteins, thereby influencing their localization, stability, and function. The relevance of FNTA in cell signaling and cancer progression has led researchers to investigate its potential as a therapeutic target. Abnormalities in protein farnesylation have been linked to various pathologies, particularly in the development of malignancies such as pancreatic cancer and other solid tumors. Due to its pivotal role in oncogenesis, inhibitors of farnesyltransferase have gained attention in drug discovery, prompting studies on FNTA's structure-function relationship, enzymatic activity, and interaction with potential drugs. Moreover, advances in recombinant protein technology enable the production and characterization of FNTA, facilitating a deeper understanding of its mechanism and interactions at the molecular level. By exploring the dynamics of FNTA and its role in cellular processes, researchers aim to unveil novel therapeutic strategies that could mitigate the impact of diseases associated with aberrant farnesylation, ultimately contributing to the development of targeted cancer therapies.
