Recombinant Human Periostin/OSF-2 (C60A) His-tag Protein, CF Summary
Details of Functionality |
Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells. The ED50 for this effect is 0.500-6.00
μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Periostin/OSF-2 protein Asn22-Gln808 (C60A) with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Asn22 |
Protein/Peptide Type |
Recombinant Proteins |
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 |
89 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 |
68-90 kDa, under reducing conditions. |
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 PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Periostin/OSF-2 (C60A) His-tag 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 human Periostin shares
91% amino acid sequence identity with mouse and rat Periostin. 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). 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). Periostin is also up-regulated in
many carcinomas (2, 8) and induces epithelial-mesenchymal transition, tumor
growth, invasion, and metastasis (9). Further, 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 up-regulated 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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