Recombinant Mouse Osteopontin/OPN Protein Summary
Details of Functionality |
Measured by the ability of the
immobilized protein to support the adhesion of HEK293 human embryonic kidney
cells. The ED50 for this effect is 0.100-1.20 µg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse Osteopontin/OPN protein Leu17-Asn294 (Glu99Gly), with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu17 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Spp1 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
31.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
30 kDa and a 65 kDa doublet, reducing conditions |
Publications |
Read Publications using 441-OP in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Osteopontin/OPN Protein
Background
Osteopontin (OPN), previously called SPP1 (secreted phosphoprotein 1), Eta-1 (early T lymphocyte activation 1) or BSP (bone sialoprotein), is a secreted molecule in the SIBLING (small integrin-binding ligand N-linked glycoprotein) family of non-collagenous matricellular proteins (1-3). Mouse OPN is synthesized as a 294 amino acid (aa) precursor protein with a 16 aa signal peptide and a 278 aa mature protein (3). Mature mouse OPN shares 79% and 64% aa sequence identity with rat and human OPN, respectively. OPN is highly acidic and has 26 potential Ser/Thr phosphorylation sites and a C‑terminal CD44 binding site (1-4). Depending on tissue-specific modification by O- and N-glycosylation, sulfation, phosphorylation and transglutamination, OPN can be detected at 45-75 kDa (5, 6). The central region of OPN contains RGD and non-RGD binding sites for multiple integrins (3, 4). Adjacent to the RGD motif is the sequence SLAYGLR (SVVYGLR in human) which serves as a cryptic binding site for additional integrins: it is masked in full length OPN but is exposed following OPN cleavage by thrombin in tumors and sites of tissue injury
(6-8). OPN can also be cleaved by MMP-3, -7, -9, and -12 within the SLAYGLR motif and at sites closer to the C-terminus (8, 9). OPN is widely expressed and is prominent in mineralized tissues. It inhibits bone mineralization and kidney stone formation, and promotes inflammation and cell adhesion and migration (1, 2, 4, 6). Its expression is up-regulated during inflammation, obesity, atherosclerosis, cancer, and tissue damage, and contributes to the pathophysiology of these conditions (1, 2, 6, 9, 10).
- Scatena, M. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:2302.
- Rangaswami, H. et al. (2006) Trends Cell Biol. 16:79.
- Miyazaki, Y. et al. (1990) J. Biol. Chem. 265:14432.
- Weber, G.F. et al. (2002) J. Leukoc. Biol. 72:752.
- Keykhosravani, M. et al. (2005) Biochemistry 44:6990.
- Kazanecki, C.C. et al. (2007) J. Cell. Biochem. 102:912.
- Senger, D.R. et al. (1994) Mol. Biol. Cell 5:565.
- Yokosaki, Y. et al. (2005) Matrix Biol. 24:418.
- Takafuji, V. et al. (2007) Oncogene 26:6361.
- Kiefer, F.W. et al. (2010) Diabetes 59:935.
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