Analytical Data
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Gene name
IGF-I R
- Application
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Alternative Names
Insulin-like growth factor I receptor ;IGF-I receptor; CD221
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Species
Human
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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
P08069
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Expression Region
763-931aa
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Protein Length
Partial
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Molecular Weight
23.4 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
Insulin-like growth factor I receptor (IGF-IR) is a critical transmembrane receptor that mediates the effects of IGF-I, a hormone influencing growth and development in various tissues. The importance of IGF-IR in cellular processes such as proliferation, differentiation, and survival has drawn significant research interest, especially in the context of cancer biology. Aberrant activation of IGF-IR signaling pathways is often associated with various malignancies, making it a potential target for therapeutic interventions. Researchers have been focusing on the development of recombinant IGF-IR proteins to study their structural and functional properties, as well as to facilitate the discovery of IGF-IR inhibitors. These recombinant proteins help in elucidating the receptor's mechanism of action, its interactions with ligands, and downstream signaling pathways. Furthermore, understanding the role of IGF-IR in diseases can lead to the development of targeted therapies, improving treatment strategies for cancer and other IGF-related disorders. The ongoing investigation into recombinant IGF-IR not only enhances our fundamental understanding of cell signaling but also opens new avenues for drug development, potentially leading to more effective treatments in combating diseases associated with IGF-IR dysregulation.
