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Periostin/OSF-2 Antibody [Biotin]

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Product Details

Summary
Applications WB, ELISA(Det)
Clonality
Polyclonal
Host
Goat
Conjugate
Biotin
Concentration
LYOPH

Order Details

Periostin/OSF-2 Antibody [Biotin] Summary

Immunogen
S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse Periostin/OSF‑2 Isoform 2
Asn24-Gln811
Accession # Q62009
Specificity
Detects mouse Periostin/OSF‑2 Isoform 2 in ELISAs and Western blots. In sandwich immunoassays, less than 0.2% cross‑reactivity with recombinant human OSF-2 is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
POSTN
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Applications/Dilutions

Application Notes
ELISA Capture: Mouse Periostin/OSF-2 Antibody (Catalog # MAB2955)
ELISA Detection: Mouse Periostin/OSF-2 Isoform 2 Biotinylated Antibody (Catalog # BAF2955)
Standard: Recombinant Mouse Periostin/OSF-2 (Catalog # 2955-F2)

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.
  • 6 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.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Background

Mouse Periostin, also known as OSF-2 (osteoblast-specific factor 2) is a 170 kDa, secreted, homodimeric protein that belongs to the periostin family of the FAS1 superfamily of molecules (1‑4). It is a TGF-beta inducible molecule that serves as both an adhesion molecule and tumor suppressor (2, 5, 6, 7). It is synthesized as a 838 amino acid (aa) precursor that contains a 23 aa signal sequence and an 815 aa mature region (2, 8). It is unknown if the molecule has any significant glycosylation (2). Based on human OSF-2, the homodimer is not disulfide-linked (3). The molecule consists of two distinct regions. The N-terminus contains an 55 aa EMI domain, while the C-terminus contains four, 130 aa fasciculin type 1 (or FAS1) domains. The EMI domain is cysteine-rich and shows a highly basic alpha -helix (9). Each FAS1 repeat exhibits a novel 7-stranded beta -wedge with a multiple alpha -helix fold (1, 8). Multiple alternate splice forms are known to exist C-terminal (aa 672‑812) to the four-fold FAS1 repeats. These mature molecules are 760, 761, 787 and 788 aa in length and show block deletions of 54 aa, 27 aa and/or 28 aa (10). The significance of the alternate splice forms is not clear. They do, however, appear to be temporally regulated (6). OSF-2 is known to bind to alpha v beta 3 and alpha v beta 5 integrins (3). It is synthesized by smooth muscle cells, fibroblasts and osteoblasts (2, 5, 7). Mature mouse OSF-2 shares 98%, 92% and 91% aa identity with rat, canine and human OSF‑2, respectively.

  1. Clout, N.J. and D. Tisi (2003) Structure 11:197.
  2. Horiuchi, K. et al. (1999) J. Bone Miner. Res. 14:1239.
  3. Gillan, L. et al. (2002) Cancer Res. 62:5358.
  4. Litvin, J. et al. (2005) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 287A:1205.
  5. Lindner, V. et al. (2005) Arterioscler. Thromb. Vasc. Biol. 25:77.
  6. Kruzynska-Frejtag, A. et al. (2004) Dev. Dyn. 229:857.
  7. Yoshioka, N. et al. (2002) Exp. Cell Res. 279:91.
  8. Takeshita, S. et al. (1993) Biochem. J. 294:271.
  9. Callebaut, I. et al. (2003) Biochem. Biophys. Res. Commun. 300:619.
  10. Swiss-Prot Accession # Q62009.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Bioinformatics

Gene Symbol POSTN