Analytical Data
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Gene name
IGF-I R
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简介
The IGF-I R protein is a receptor tyrosine kinase that mediates the effects of insulin-like growth factor 1 (IGF1) and has high affinity for IGF1. Upon ligand binding, IGF1R is activated, leading to autophosphorylation and tyrosine phosphorylation of substrates, including IRS1/2, Shc, and 14-3-3 proteins. IGF-I R Protein, Mouse (HEK293, His) is the recombinant mouse-derived IGF-I R protein, expressed by HEK293 , with C-His labeled tag.
- Application
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Biological Activity
1. Immobilized Mouse IGF1R, His Tag at 1 μg/mL (100 μl/well) on the plate. Dose response curve for Human IGFI, hFc Tag with the EC50 of 2.58 μg/mL determined by ELISA. 2.Measured by its binding ability in a functional ELISA. When Recombinant Mouse IGF-I R is immobilized at 5 µg/mL (100 µL/well) can bind Recombinant Human IGF-I. The ED50 for this effect is 322.3 ng/mL. Measured by its binding ability in a functional ELISA. When Recombinant Mouse IGF-I R is immobilized at 5 µg/mL (100 µL/well) can bind Recombinant Human IGF-I. The ED50 for this effect is 322.3 ng/mL.
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Alternative Names
IGF1R; IGFR; JTK13; CD221; MGC142170; MGC142172; MGC18216
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Species
Mouse
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
Q60751-1
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Expression Region
E31-H936
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AA Sequence
EICGPGIDIRNDYQQLKRLENCTVIEGFLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTIDWSLILDAVSNNYIVGNKPPKECGDLCPGTLEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSVCGKRACTENNECCHPECLGSCHTPDDNTTCVACRHYYYKGVCVPACPPGTYRFEGWRCVDRDFCANIPNAESSDSDGFVIHDDECMQECPSGFIRNSTQSMYCIPCEGPCPKVCGDEEKKTKTIDSVTSAQMLQGCTILKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWNHRNLTVRSGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLRFTSTTTWKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKEGEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDVEEVTENPKTEVCGGDKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERRRRDVMQVANTTMSSRSRNTTVADTYNITDPEEFETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVPAKTTYENFMH
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Protein Length
Partial
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Molecular Weight
110-140 & 50-65 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 protein in cell signaling pathways that regulates growth, development, and metabolism. It is a transmembrane glycoprotein that belongs to the receptor tyrosine kinase family and is activated by its ligands, IGF-I and IGF-II. The importance of IGF-IR is underscored by its role in cellular processes such as proliferation, differentiation, and survival, making it a key player in various physiological and pathological conditions, including cancer and metabolic disorders. Research on recombinant IGF-IR proteins has gained momentum due to their potential applications in therapeutic interventions and drug development. By producing recombinant IGF-IR, scientists can study its structure, function, and interactions in detail, facilitating the identification of inhibitors that can modulate its activity in disease contexts. Furthermore, understanding the signaling pathways associated with IGF-IR can lead to novel strategies for targeting tumors that exhibit aberrant IGF signaling. Given the receptor's involvement in promoting tumorigenesis, harnessing recombinant IGF-IR for high-throughput screening of small molecules represents a promising approach in cancer therapy. Overall, the investigation of recombinant IGF-IR proteins not only enhances our understanding of fundamental biological mechanisms but also aids in the development of innovative treatments for diseases linked to dysregulated IGF signaling.
