Analytical Data
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基因名
Igflr1
- Application
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别名
(Transmembrane protein 149)
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种属
Mouse
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表达系统
E. coli
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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
Q3U4N7
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表达区间
21-163aa
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分子量
19.3 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
IGFLR1 (Insulin-like Growth Factor Binding Protein-like 1 Receptor) is a unique receptor that plays a crucial role in cellular growth, differentiation, and survival pathways, particularly in the context of cancer and developmental biology. The study of IGFLR1 has gained significance due to its involvement in modulating the actions of insulin-like growth factors (IGFs), which are essential for various physiological processes. Disruptions in IGF signaling have been linked to numerous diseases, including obesity, diabetes, and various malignancies. Research on IGFLR1 reconstituted proteins aims to elucidate the receptor's structure-function relationships, its ligand interactions, and downstream signaling mechanisms. Understanding IGFLR1 at the molecular level may offer insights into targeted therapies that can manipulate IGF signaling pathways for clinical benefit. Additionally, IGFLR1's potential as a biomarker for certain cancers and its implications in metabolic disorders make it a compelling subject for further investigation. Overall, the exploration of IGFLR1, including its recombinant protein, holds promise for advancing therapeutic strategies and improving our understanding of IGF-related pathological conditions.
