Recombinant Human Osteoadherin Protein, CF Summary
Details of Functionality
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 human Osteoadherin/OSAD protein Gln21-Glu421, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
47.9 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
60-66 kDa, reducing conditions
Publications
Read Publication using 2884-AD in the following applications:
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 reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human 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 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).
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.
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