Analytical Data
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Gene name
Osteopontin
- Application
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Alternative Names
SPP1;BNSP;OPN;Osteopontin
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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
P10451
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Expression Region
17-314aa
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AA Sequence
IPVKQADSGS SEEKQLYNKY PDAVATWLNP DPSQKQNLLA PQNAVSSEET NDFKQETLPS KSNESHDHMD DMDDEDDDDH VDSQDSIDSN DSDDVDDTDD SHQSDESHHS DESDELVTDF PTDLPATEVF TPVVPTVDTY DGRGDSVVYG LRSKSKKFRR PDIQYPDATD EDITSHMESE ELNGAYKAIP VAQDLNAPSD WDSRGKDSYE TSQLDDQSAE THSHKQSRLY KRKANDESNE HSDVIDSQEL SKVSREFHSH EFHSHEDMLV VDPKSKEEDK HLKFRISHEL DSASSEVN
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Molecular Weight
34 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
Osteopontin (OPN) is a glycoprotein that plays a crucial role in various physiological and pathological processes, including bone remodeling, immune response, and tissue regeneration. Originally identified in bone, OPN is also expressed in many other tissues, indicating its diverse functions beyond skeletal health. Research has shown that OPN participates in cell adhesion, migration, and signaling pathways, which are essential for processes like inflammation and tumor progression. Given its importance in these biological processes, OPN has garnered attention as a potential therapeutic target for various diseases, including osteoporosis, cancer, and cardiovascular diseases. The recombinant form of OPN has been developed and characterized to enable detailed studies of its biological functions and interactions at the molecular level. Additionally, recombinant OPN can serve as a valuable tool for investigating its role in cell signaling and the immune system, providing insights that could lead to novel therapeutic strategies. Understanding the structure-function relationship of OPN through recombinant technology not only enhances our fundamental knowledge of its biology but also opens new avenues for clinical applications, such as developing biomaterials for bone repair or modulating immune responses in diseases. Overall, research on recombinant OPN holds promise for advancing both basic science and translational medicine, making it a significant focus in biomedical research.
