Analytical Data
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Gene name
IGFBP-7
- Application
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Alternative Names
FSTL2; IGFBP-7v; MAC25; PSF; TAF; IGFBP-rP1; MAC25 protein; Prostacyclin-stimulating factor; PGI2-stimulating factor; Tumor-derived adhesion factor
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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 85% as determined by SDS-PAGE.
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Uniprot
Q16270
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Expression Region
Ser27~Leu282
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Protein Length
Partial
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Molecular Weight
35kDa
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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 Binding Protein-7 (IGFBP-7) is a member of the IGFBP family, which plays a crucial role in regulating the bioavailability of insulin-like growth factors (IGFs) that are pivotal in cellular growth, differentiation, and metabolism. Research has indicated that IGFBP-7 exhibits multifaceted functions beyond its binding abilities, such as modulating apoptosis, playing a role in tumorigenesis, and influencing tissue repair processes. Elevated levels of IGFBP-7 have been implicated in various pathological conditions, including cancer, cardiovascular diseases, and metabolic disorders. The recombinant production of IGFBP-7 has been explored to elucidate its biological functions and therapeutic potential. By generating pure IGFBP-7 protein, researchers aim to investigate its effects on cellular pathways and its potential as a biomarker for disease prognosis or as a target for novel therapeutic strategies. Moreover, understanding the structure-function relationship of IGFBP-7 can facilitate the development of IGFBP-7-based drugs or therapies, highlighting its significance in both fundamental and clinical research. The ongoing studies into IGFBP-7's mechanisms of action continue to unravel its potential roles in health and disease, making it a compelling subject of investigation in the fields of endocrinology, oncology, and regenerative medicine.











