Analytical Data
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基因名
GIGYF2
- Application
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别名
GRB10-interacting GYF protein 2Trinucleotide repeat-containing gene 15 protein
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种属
Human
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表达系统
Yeast
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6Y7W6
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表达区间
510-1030aa
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分子量
64.6 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
