Recombinant Human Osteoadherin Protein, CF Summary
Gln21-Glu421, with a C-terminal 6-His tag
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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.
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||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile 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.
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 human OSAD cDNA encodes a 421 aa precursor that contains a 20 aa signal sequence and eleven tandem leucine rich repeats (3). Human OSAD shares 80 - 84% aa sequence identity with bovine, mouse, and rat OSAD. Human OSAD shares 32 - 35% aa sequence identity with human class II SLRPs Fibromodulin, Keratocan, Lumican, and PRELP. Bovine, mouse, and rat OSAD are expressed as 60 - 85 kDa molecules, although 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 also 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).
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- Kobe, B. and A.V. Kajava (2001) Curr. Opin. Struct. Biol. 11:725.
- Sommarin, Y. et al. (1998) J. Biol. Chem. 273:16723.
- Wendel, M. et al. (1998) J. Cell Biol. 141:839.
- Hultenby, P.U. et al. (2003) Eur. J. Oral Sci. 111:128.
- Lucchini, M. et al. (2004) J. Dent. Res. 83:552.
- Onnerfjord, P. et al. (2004) J. Biol. Chem. 279:26
- Shen, Z. et al. (1999) Matrix Biol. 18:533.
- Buchaille, R. et al. (2000) Bone 27:265.
- Buchaille, R. et al. (2000) Matrix Biol. 19:421.
- Couble, M.L. et al. (2004) Histochem. Cell Biol. 121:47.
- Ramstad, V.E. et al. (2003) Calcif. Tissue Int. 72:57.
Citation for Recombinant Human 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
Comparison of secretome from osteoblasts derived from sclerotic versus non-sclerotic subchondral bone in OA: A pilot study
Authors: C Sanchez, G Mazzucchel, C Lambert, F Comblain, E DePauw, Y Henrotin
PLoS ONE, 2018;13(3):e0194591.
Sample Types: Cell Culture Supernates
Applications: Western Blot
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