Analytical Data
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Gene name
Igflr1
- Application
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Alternative Names
(Transmembrane protein 149)
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Species
Mouse
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Source
E. coli
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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
Q3U4N7
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Expression Region
21-163aa
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Molecular Weight
19.3 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
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.
