Detects mouse Osteoadherin/OSAD in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 10% cross-reactivity with recombinant human OSAD is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
OMD
Purity Statement
Antigen Affinity-purified
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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. 6 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Osteoadherin/OSAD/OMD Antibody [Unconjugated]
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).
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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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