Analytical Data
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Gene name
IGFBP3
- Application
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Alternative Names
IGFBP3；IBP3；Insulin-like growth factor-binding Protein 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17936
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Expression Region
28-291aa
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AA Sequence
GGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK
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Molecular Weight
29 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 binding protein 3 (IGFBP3) is a critical regulator of the insulin-like growth factor (IGF) signaling pathway, which plays a vital role in cellular growth, development, and apoptosis. As the most abundant IGFBP in circulation, IGFBP3 not only modulates IGF activity but also has IGF-independent effects, influencing cell adhesion, matrix interaction, and apoptosis in various tissues. Dysregulation of IGFBP3 has been associated with numerous diseases, including cancer, diabetes, and cardiovascular disorders, making it a significant focus of research. The recombinant production of IGFBP3 in various expression systems, including bacterial, yeast, and mammalian cells, has facilitated a more profound understanding of its biological functions and therapeutic potential. Recent studies have explored IGFBP3's roles in tumor biology, revealing that it can act as a tumor suppressor in certain contexts while promoting proliferation and invasion in others, depending on the cellular environment and the presence of IGFs. Additionally, IGFBP3 is being investigated as a potential biomarker for disease diagnosis and prognosis, particularly in oncology. The development of recombinant IGFBP3 not only aids in elucidating its physiological roles but also paves the way for potential clinical applications, including targeted therapies and novel treatment strategies for diseases linked to IGF signaling dysregulation. Understanding the structure-function relationship of IGFBP3 through recombinant technologies is crucial for harnessing its therapeutic potential and addressing various pathologies associated with altered IGF signaling.
