Recombinant Mouse Osteoadherin Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Citations (1)

Recombinant Mouse Osteoadherin Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to modulate collagen fibrillogenesis. Ge, G. et al. (2004) J. Biol. Chem. 279:41626. At 5 µg/mL, rmOSAD can significantly enhance the rate of type I collagen fibrillogenesis.
Mouse myeloma cell line, NS0-derived mouse Osteoadherin/OSAD protein
Gln21-Ile423, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln21 predicted
Structure / Form
Predicted Molecular Mass
48.2 kDa
66-76 kDa, reducing conditions

Product Datasheets

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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.


Formulation Supplied as a 0.2 μm filtered solution in PBS.
Shipping The product is shipped with dry ice or equivalent. 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 opening.
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Background: Osteoadherin/OSAD

Osteoadherin (OSAD), also known as Osteomodulin, is an extracellular matrix keratan sulfate proteoglycan that belongs to the class II subfamily of small leucine-rich proteoglycans (SLRP). LRR motifs consist of approximately 20 - 30 amino acids (aa) with conserved leucine spacing, folded into a structure with one beta -sheet and one alpha -helix (1, 2). The mouse OSAD cDNA encodes a 423 aa precursor that contains a 20 aa signal sequence and twelve tandem leucine rich repeats (3). Mouse OSAD shares 75%, 79%, and 91% aa sequence identity with bovine, human, and rat OSAD, respectively. Mouse OSAD shares 32 - 35% aa sequence identity with mouse class II SLRPs Fibromodulin, Keratocan, Lumican, and PRELP. Bovine, mouse, and rat OSAD are expressed as 60 - 85 kDa molecules, even though the amino acid sequence for each predicts a size of 46 - 47 kDa. The primary difference is due to the presence of extensive N-linked glycosylation that can vary between tissues of the same species (4, 5). Human OSAD is expressed as an even larger 110 kDa molecule in teeth (6). OSAD contains eight sulfated tyrosine residues (4, 7) and is distinguished from other class II SLRPs by the presence of an approximately 70 aa C-terminal acidic domain (3). OSAD is expressed by fetal and adult osteoblasts but is not detectable in cartilage or tendon (3, 4, 8). In dental tissue, OSAD is expressed by odontoblasts and ameloblasts (5, 9 - 11) and is involved in the mineralization of bone and teeth (5, 11,12). OSAD promotes the adhesion of osteoblasts and odontoblasts to the surrounding matrix, an interaction that is mediated by Integrin alpha V beta 3 (4, 6).

  1. Matsushima, N. et al. (2000) Proteins 38:210.
  2. Kobe, B. and A.V. Kajava (2001) Curr. Opin. Struct. Biol. 11:725.
  3. Sommarin, Y. et al. (1998) J. Biol. Chem. 273:16723.
  4. Wendel, M. et al. (1998) J. Cell Biol. 141:839.
  5. Hultenby, P.U. et al. (2003) Eur. J. Oral Sci. 111:128.
  6. Lucchini, M. et al. (2004) J. Dent. Res. 83:552.
  7. Onnerfjord, P. et al. (2004) J. Biol. Chem. 279:26.
  8. Shen, Z. et al. (1999) Matrix Biol. 18:533.
  9. Buchaille, R. et al. (2000) Bone 27:265.
  10. Buchaille, R. et al. (2000) Matrix Biol. 19:421.
  11. Couble, M.L. et al. (2004) Histochem. Cell Biol. 121:47.
  12. Ramstad, V.E. et al. (2003) Calcif. Tissue Int. 72:57.
Entrez Gene IDs
4958 (Human)
Alternate Names
Keratan sulfate proteoglycan osteomodulin; KSPG osteomodulin; OMD; OSAD; osteoadherin proteoglycan; Osteoadherin; osteomodulin; SLRR2C; SLRR2Costeoadherin

Citation for Recombinant Mouse Osteoadherin 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. Osteoadherin accumulates in the predentin towards the mineralization front in the developing tooth.
    Authors: Nikdin H, Olsson ML, Hultenby K
    PLoS ONE, 2012;7(2):e31525.
    Species: N/A
    Sample Types: N/A
    Applications: Antibody Absorption


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