Analytical Data
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Gene name
GFER
- Application
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Alternative Names
GFER；ALR；HERV1；TRC35;FAD-linked sulfhydryl oxidase ALR
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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
P55789-1
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Expression Region
1-125aa
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AA Sequence
MAAPGERGRF HGGNLFFLPG GARSEMMDDL ATDARGRGAG RRDAAASAST PAQAPTSDSP VAEDASRRRP CRACVDFKTW MRTQQKRDTK FREDCPPDRE ELGRHSWAVL HTLAAYYPDL PTPEQ
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Molecular Weight
17 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
The GFER (Glutaredoxin-Expressed Protein in Redox Biology) recombinant protein has garnered significant attention in recent years due to its critical role in cellular redox signaling and the regulation of oxidative stress. Research has advanced our understanding of how GFER contributes to the maintenance of cellular homeostasis, particularly in the context of various diseases, including neurodegenerative disorders and cancer. Given the oxidative environment of many cellular processes, GFER acts as an important mediator, facilitating the reduction of disulfide bonds in proteins and maintaining the thiol redox state within cells. Recombinant expression of GFER allows for the production of pure, functional protein for biochemical and structural studies, shedding light on its mechanisms of action and potential therapeutic applications. Investigating the interactions of GFER with other cellular components has implications for developing targeted therapies that harness its protective effects against oxidative damage. Furthermore, understanding the nuances of GFER’s function in redox biology can pave the way for novel strategies to combat diseases characterized by elevated oxidative stress, thus underscoring the importance of this research in both fundamental biology and translational medicine.
