Analytical Data
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Gene name
NOV/CCN3
- Application
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Alternative Names
NovH, Insulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P48745
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Expression Region
28-357aa
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Molecular Weight
36.2 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
NOV (Nephroblastoma Overexpressed) and CCN3 (Cellular Communication Network Factor 3) are members of the CCN family of proteins, which play crucial roles in cellular processes such as proliferation, differentiation, and tissue repair. NOV, initially identified as an oncofetal protein, is known for its upregulation in various cancers, including nephroblastoma, suggesting its potential role in tumorigenesis. On the other hand, CCN3 has been implicated in bone development and regulation of cell-matrix interactions, with expression patterns that indicate significant involvement in both normal physiology and pathological conditions. Research into the functional properties of NOV and CCN3, particularly their interactions and signaling pathways, has garnered interest due to their potential as therapeutic targets. Understanding the mechanisms through which NOV and CCN3 influence cell behavior, particularly in the context of cancer and tissue regeneration, is crucial for developing novel strategies in regenerative medicine and oncology. Recent studies have focused on their synergistic effects on cell migration, survival, and ECM (extracellular matrix) interactions, further elucidating their roles in the tumor microenvironment. Overall, the investigation of NOV/CCN3 recombinant proteins is expanding our knowledge of cell communication and may lead to innovative interventions for cancer treatment and regenerative therapies.
