Recombinant Mouse Osteoadherin Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Osteoadherin Protein, CF Summary

• Details of Functionality: 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.
• Source: Mouse myeloma cell line, NS0-derived mouse Osteoadherin/OSAD protein Gln21-Ile423, with a C-terminal 6-His tag
• Accession #: O35103
• N-terminal Sequence: No results obtained: Gln21 predicted
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 48.2 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: 66-76 kDa, 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

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

Alternate Names for Recombinant Mouse Osteoadherin Protein, CF

• Keratan sulfate proteoglycan osteomodulin
• KSPG osteomodulin
• OMD
• OSAD
• osteoadherin proteoglycan
• Osteoadherin
• osteomodulin
• SLRR2C
• SLRR2Costeoadherin

Background

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.

Publications for Osteoadherin/OSAD/OMD (3308-AD)(1)

Publication using 3308-AD

• Nikdin H, Olsson ML, Hultenby K Osteoadherin accumulates in the predentin towards the mineralization front in the developing tooth. PLoS ONE, 2012-02-15;7(2):e31525. 2012-02-15 [PMID: 22355375] (Antibody Absorption)

Bioinformatics

• Uniprot:
  • O35103()