Analytical Data
-
Gene name
Osteopontin/OPN
-
简介
Osteopontin/OPN Protein, a key non-collagenous bone protein, strongly binds to hydroxyapatite, crucial for the mineralized matrix.It likely plays a vital role in mediating cell-extracellular matrix interactions.Additionally, as a cytokine, OPN stimulates interferon-gamma and interleukin-12 production, while inhibiting interleukin-10, pivotal for the type I immunity pathway.Osteopontin/OPN Protein, Rat (CHO, His) is the recombinant rat-derived Osteopontin/OPN protein, expressed by CHO , with C-6*His labeled tag.
- Application
-
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. When 1 x 10^5 cells/well are added to Recombinant Rat Osteopontin/OPN coated plates, cell adhesion is enhanced in a dose dependent manner after 1 hour incubation at 37°C. The ED50 for this effect is < 1.50 µg/mL. Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. When 1 x 105 cells/well are added to Recombinant Rat Osteopontin/OPN coated plates, cell adhesion is enhanced in a dose dependent manner after 1 hour incubation at 37°C. The ED50 for this effect is 1.281 μg/ml, corresponding to a specific activity is 780.640 units/mg.
-
Alternative Names
Osteopontin; Spp1; Bone sialoprotein 1; Secreted phosphoprotein 1; SPP-1; 2b7; Secreted Phosphoprotein 1 [BNSP]
-
Species
Rat
-
Source
CHO
-
Tag
C-6*His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P08721
-
Expression Region
L17-N317
-
AA Sequence
LPVKVAEFGSSEEKAHYSKHSDAVATWLKPDPSQKQNLLAPQNSVSSEETDDFKQETLPSNSNESHDHMDDDDDDDDDGDHAESEDSVNSDESDESHHSDESDESFTASTQADVLTPIAPTVDVPDGRGDSLAYGLRSKSRSFPVSDEQYPDATDEDLTSRMKSQESDEAIKVIPVAQRLSVPSDQDSNGKTSHESSQLDEPSVETHSLEQSKEYKQRASHESTEQSDAIDSAEKPDAIDSAERSDAIDSQASSKASLEHQSHEFHSHEDKLVLDPKSKEDDRYLKFRISHELESSSSEVN
-
Protein Length
Full Length of Mature Protein
-
Molecular Weight
Predict MW: 34.83 kDa; 60-70 kDa band in SDS-PAGE under reducing conditions
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 cellular adhesion. Initially identified as a component of the bone matrix, OPN has since been implicated in a range of diseases, including cancer, cardiovascular disorders, and chronic inflammatory conditions. The ability of OPN to interact with various cell types through its multiple binding sites facilitates its involvement in cellular signaling pathways, making it a valuable target for therapeutic intervention. Recent research has focused on the production and characterization of recombinant OPN proteins to better understand its biological functions and mechanisms of action. Recombinant OPN proteins enable researchers to elucidate the specific roles of OPN in cell adhesion, migration, and tissue remodeling, providing insights into its potential as a biomarker for disease progression and as a therapeutic target. Furthermore, the study of OPN's interactions with other proteins and its post-translational modifications is essential for developing novel strategies to modulate its activity in various clinical contexts. As such, ongoing investigations into the structure, function, and applications of recombinant osteopontin proteins continue to shed light on their significance in health and disease.











