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. Recombinant Human Osteoadherin, immobilized at 20 µg/mL (100 µL/well) can induce more than 35% of ATDC-5 cell adhesion.
Source
Mouse myeloma cell line, NS0-derived Gln21-Glu421, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
AnalysisNo results obtained: Gln21 predicted
Predicted Molecular Mass
47.9 kDa
SDS-PAGE
60-66 kDa, reducing conditions
2884-AD |
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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.
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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 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).
References:
Matsushima, N. et al. (2000) Proteins 38:210.
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.
Entrez Gene IDs:
4958 (Human)
Alternate Names:
Keratan sulfate proteoglycan osteomodulin; KSPG osteomodulin; OMD; OSAD; osteoadherin proteoglycan; Osteoadherin; osteomodulin; SLRR2C; SLRR2Costeoadherin
