Analytical Data
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Gene name
IGFBP-3
- Application
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Alternative Names
BP53; IBP3; Growth Hormone-Dependent Binding Protein; Acid Stable Subunit Of The 140 K IGF Complex
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Species
Mouse
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Source
HEK293
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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
P47878
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Expression Region
Ser152~Gln292
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Molecular Weight
17kDa
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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 binding protein 3 (IGFBP-3) is a key regulator of insulin-like growth factor (IGF) actions, playing a critical role in cellular growth, differentiation, and apoptosis. It binds to IGF with high affinity, modulating its bioavailability and activity in various physiological contexts. Given its significant involvement in cancer biology, particularly in tumor growth and metastasis, IGFBP-3 has garnered attention as a potential therapeutic target. Research has shown that alterations in IGFBP-3 levels are associated with various malignancies, emphasizing its importance in cancer prognosis and treatment. Moreover, recombinant forms of IGFBP-3 are being explored for therapeutic applications due to their ability to inhibit tumor cell proliferation and induce apoptosis in cancerous cells. The production of recombinant IGFBP-3 allows for high-purity preparations for in vitro and in vivo studies, facilitating insights into its biological functions and mechanisms of action. As researchers continue to delineate the pathways affected by IGFBP-3, its potential as a biotherapeutic agent is becoming increasingly apparent, opening avenues for innovative cancer treatments. Understanding the biology of IGFBP-3 not only enhances our grasp of IGF signaling but also presents opportunities for novel interventions in diseases linked to IGF dysregulation, thereby underlining the importance of ongoing research in this critical field.
