Analytical Data
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Gene name
GIGYF2
- Application
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Alternative Names
GRB10-interacting GYF protein 2Trinucleotide repeat-containing gene 15 protein
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6Y7W6
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Expression Region
510-1030aa
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Molecular Weight
64.6 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
Related Products
Protein Description
GIGYF2 (Grb10-Interacting GYF Protein 2) is a notable member of the GYF protein family, which plays critical roles in various cellular processes, including mRNA stability, translation regulation, and protein-protein interactions. Recent research has highlighted GIGYF2's involvement in signaling pathways affecting cell growth and proliferation, as well as its potential roles in neurodevelopment and cancer biology. Given its interactions with significant signaling proteins and its influence on mTOR (mechanistic target of rapamycin) signaling, GIGYF2 is being investigated for its functional implications in metabolic disorders and tumors. The recombinant expression of GIGYF2 in various systems facilitates the study of its biochemical properties and intricate mechanisms of action. Understanding GIGYF2’s structure-function relationship is crucial for elucidating its role in pathophysiological conditions, which may lead to novel therapeutic strategies targeting diseases where GIGYF2 is implicated. As the field advances, producing and characterizing GIGYF2 as a recombinant protein offers insights into its biological functions and potential applications in biotechnology and medicine.
