Recombinant Mouse Periostin/OSF-2 Protein, CF Summary
Details of Functionality |
Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells. Immobilized Recombinant Mouse Periostin/OSF‑2 at 10 µg/mL (100 µL/well) induces >50% cell adhesion. |
Source |
Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse Periostin/OSF-2 protein Asn24-Gln811, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Asn24 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Postn |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
88.5 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 |
90 kDa, reducing conditions |
Publications |
Read Publications using 2955-F2 in the following applications:
|
|
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.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Periostin/OSF-2 Protein, CF
Background
Periostin, also known as OSF-2, is a secreted matricellular protein with functions in extracellular matrix formation, cell migration, and inflammation (1). It is secreted as a 90 kDa monomer that can aggregate into >170 kDa higher-order multimers (2). Periostin contains an N-terminal EMI domain followed by four tandem FAS1 domains (3). Mature mouse Periostin shares 91% and 98% aa sequence identity with mouse and rat Periostin, respectively. Alternative splicing generates additional isoforms with various deletions in the C-terminal region following the FAS domains. Periostin is expressed by mesenchymal cells such as vascular smooth muscle cells, fibroblasts, osteoblasts, and odontoblasts in developing teeth (4-7). It is up-regulated in many carcinomas (2, 8). Periostin binds to Integrins alpha
v beta
3 and alpha
v beta
5 (2, 9), leading to enhanced cell adhesion and cell migration (2, 5, 6). It enhances Fibronectin and Collagen I production and promotes collagen fibrillogenesis (10, 11). It also induces epithelial-mesenchymal transition, tumor growth, invasion, and metastasis (9). Periostin induces the expression of VEGF R2 on endothelial cells and VEGF-C in tumor cells, and it can induce tumor lymphangiogenesis (8, 12). Periostin plays an important role in heart valve development and tissue healing after myocardial infarction (5, 13, 14). In asthma, it is upregulated in bronchial epithelium and plays both destructive and protective roles by inducing eosinophil infiltration and inhibiting goblet cell metaplasia and mucus production, respectively (15, 16).
- Liu, A.Y. et al. (2014) Matrix Biol. 37:150.
- Gillan, L. et al. (2002) Cancer Res. 62:5358.
- Takeshita, S. et al. (1993) Biochem. J. 294:271.
- Kruzynska-Frejtag, A. et al. (2004) Dev. Dyn. 229:857.
- Lindner, V. et al. (2005) Arterioscler. Thromb. Vasc. Biol. 25:77.
- Horiuchi, K. et al. (1999) J. Bone Miner. Res. 14:1239.
- Li, G. et al. (2006) Atherosclerosis 188:292.
- Shao, R. et al. (2004) Mol. Cell. Biol. 24:3992.
- Yan, W. and R. Shao (2006) J. Biol. Chem. 281:19700.
- Erkan, M. et al. (2007) Gastroenterology 132:1447.
- Norris, R.A. et al. (2007) J. Cell. Biochem. 101:695.
- Kudo, Y. et al. (2012) PLoS One 7:e44488.
- Snider, P. et al. (2008) Circ. Res. 102:752.
- Kuhn, B. et al. (2007) Nat. Med. 13:962.
- Blanchard, C. et al. (2008) Mucosal Immunol. 1:289.
- Sehra, S. et al. (2011) J. Immunol. 186:4959.
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