Analytical Data
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Gene name
IGF-I R
- Application
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Alternative Names
Insulin-like growth factor I receptor Short name: IGF-I receptor
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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
P08069
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Expression Region
763-931aa
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Molecular Weight
21.4 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
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Protein Description
Insulin-like Growth Factor I Receptor (IGF-IR) plays a crucial role in cell growth, differentiation, and survival, making it a key player in various physiological processes and diseases, particularly cancer. The receptor is activated by its ligand, IGF-I, leading to a cascade of signaling pathways that promote cellular proliferation and inhibit apoptosis. In recent years, research has increasingly focused on the role of IGF-IR in tumorigenesis, as its overexpression is often associated with enhanced tumor growth, metastasis, and resistance to therapies. Consequently, IGF-IR presents a promising target for therapeutic interventions, with recombinant proteins engineered to disrupt its function being explored as potential cancer treatments. These recombinant proteins can function as antagonists to block IGF-IR signaling or as monoclonal antibodies designed to inhibit receptor activation and downstream signaling pathways. Additionally, understanding the structure and function of IGF-IR through recombinant protein studies offers insights into its mechanism and interactions, laying the groundwork for developing novel drugs aimed at modulating its activity. Overall, the study of IGF-IR recombinant proteins not only enhances our knowledge of cellular mechanisms underlying various diseases but also contributes to the advancement of targeted therapies in oncology.
