Recombinant Rat Periostin/OSF-2 Protein, CF

Newer Version Available: 11253-F2
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8994-F2-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Rat Periostin/OSF-2 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells. The ED50 for this effect is 0.6-3.6 µg/mL.
Source
Human embryonic kidney cell, HEK293-derived rat Periostin/OSF-2 protein
Asn24-Ser800, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Asn24
Predicted Molecular Mass
87 kDa
SDS-PAGE
77-95 kDa, reducing conditions

Product Datasheets

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8994-F2

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

8994-F2

Formulation Lyophilized from a 0.2 μm filtered solution in MES, NaCl and Brij-35.
Reconstitution Reconstitute at 500 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: Periostin/OSF-2

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). Alternative splicing generates additional isoforms of rat Periostin with various deletions in the C-terminal region following the FAS domains. This recombinant protein corresponds to the isoform of rat Periostin that lacks aa 785-812. It shares 90% and 97% aa sequence identity with comparable isoforms of human and mouse Periostin, respectively. 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 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).

References
  1. Liu, A.Y. et al. (2014) Matrix Biol. 37:150.
  2. Gillan, L. et al. (2002) Cancer Res. 62:5358.
  3. Takeshita, S. et al. (1993) Biochem. J. 294:271.
  4. Kruzynska-Frejtag, A. et al. (2004) Dev. Dyn. 229:857.
  5. Lindner, V. et al. (2005) Arterioscler. Thromb. Vasc. Biol. 25:77.
  6. Horiuchi, K. et al. (1999) J. Bone Miner. Res. 14:1239.
  7. Li, G. et al. (2006) Atherosclerosis 188:292.
  8. Shao, R. et al. (2004) Mol. Cell. Biol. 24:3992.
  9. Yan, W. and R. Shao (2006) J. Biol. Chem. 281:19700.
  10. Erkan, M. et al. (2007) Gastroenterology 132:1447.
  11. Norris, R.A. et al. (2007) J. Cell. Biochem. 101:695.
  12. Kudo, Y. et al. (2012) PLoS One 7:e44488.
  13. Snider, P. et al. (2008) Circ. Res. 102:752.
  14. Kuhn, B. et al. (2007) Nat. Med. 13:962.
  15. Blanchard, C. et al. (2008) Mucosal Immunol. 1:289.
  16. Sehra, S. et al. (2011) J. Immunol. 186:4959.
Long Name
Osteoblast Specific Factor 2
Entrez Gene IDs
10631 (Human); 50706 (Mouse); 361945 (Rat)
Alternate Names
Fasciclin I-like; MGC119510; MGC119511; OSF2; OSF-2; OSF-2osteoblast specific factor 2 (fasciclin I-like); OSF2periodontal ligament-specific periostin; Osteoblast-specific factor 2; PDLPOSTN; periostin isoform thy2; periostin isoform thy4; periostin isoform thy6; periostin isoform thy8; Periostin; periostin, osteoblast specific factor; PNRP11-412K4.1; POSTN; TRIF52

Citation for Recombinant Rat Periostin/OSF-2 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. POSTN promotes diabetic vascular calcification by interfering with autophagic flux
    Authors: XJ Sun, WQ Ma, Y Zhu, NF Liu
    Cellular Signalling, 2021-03-17;0(0):109983.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay

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