Osteoadherin

Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (αvβ3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847). abstract = "Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone.

Osteoadherin, fibromodulin, and chondroadherin, which bind C1q and activate complement, were found to cause significantly higher C9 deposition in C4BP-depleted serum compared with Igs, indicating that the level of complement activation initiated by SLRPs is regulated by simultaneous binding to C4BP. Osteoadherin/OSAD/OMD Polyclonal antibody specifically detects Osteoadherin/OSAD/OMD in Human, Mouse, Rat, Porcine, Bovine, Canine, Equine, Guinea Pig, Rabbit, Zebrafish samples. It … 2012-02-15 Osteoadherin (B-10) is a mouse monoclonal antibody raised against amino acids 221-380 mapping within an internal region of Osteoadherin of human origin. PRODUCT Each vial contains 200 µg IgG 1 kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin. Osteoadherin (B-10) is available conjugated to agarose (sc-271102 AC), 2003-12-12 Sommarin Y, Wendel M, Shen Z, Hellman U, Heinegard D (1998) Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix.

Leucine-rich repeat (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.

Every product we sell is backed by Novus' 100% Guarantee.If you have used this product, please submit your images and reviews to earn reward points. Sommarin Y, Wendel M, Shen Z, Hellman U, Heinegard D (1998) Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix. J Biol Chem 273:16723–16729 PubMed CrossRef Google Scholar 2012-02-15 · Osteoadherin (OSAD), a 47 kDa KS-SLRP, was identified and purified from bovine long bones by Wendel et al.

ELISA detected osteoadherin in bovine bone only, and immunohistochemical analysis of bovine fetal rib growth plate showed osteoadherin exclusively in primary bone spongiosa. A: Chelating agents such as EDTA, Heparin and Citrate can bind metal ions from the functional domain of Osteoadherin causing degradation of its protein structure.

In bone Aug 6, 2009 Transforming growth factor beta 1 (TGF g 1) is generally considered to be a potent inducer of dentin formation. In order to further assess this Recently, osteoadherin (OSAD) has been described as a new member of this family, that is expressed by mature bovine osteoblasts.
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An important paralog of this gene is KERA.

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The human protein, encoded by the gene OMD, is 421 amino acid residues long and has a mass of 49,492 daltons. It is a member of the Small leucine-rich proteoglycan (SLRP) family, SLRP class II subfamily. This protein is reported to have a secreted cellular Anti-OMD antibody produced in rabbit Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody; Synonym: SLRR2C, osteoadherin; find Sigma-Aldrich-HPA069948 MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich. Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone. Based on results obtained from in vitro experiments, the protein was shown to bind osteoblasts via the integrin receptor alpha(v)beta(3).

J Biol Chem 273:16723–16729 PubMed CrossRef Google Scholar Transforming growth factor beta 1 (TGF g 1) is generally considered to be a potent inducer of dentin formation. In order to further assess this role, we studied the influence of this factor in human dental pulp cells on the expression of osteoadherin (OSAD), a newly described proteoglycan found in bone and dentin and suspected to play a role in mineralization events. Osteoadherin (OSAD), also known as Osteomodulin, is an extracellular matrix keratan sulfate proteoglycan that belongs to the class II subfamily of small leucinerich proteoglycans (SLRP).

1998-05-01 · In addition, pure osteoadherin was shown not to react with antisera against other acidic glycoproteins from bone matrix such as osteonectin, osteopontin, bone sialoprotein, decorin, or biglycan. Osteoadherin seems to be restricted to bone as assayed by an inhibition ELISA. Other proteins exclusively restricted to bone include osteocalcin and BSP. The small leucine-rich repeat proteins (SLRPs), fibromodulin and osteoadherin, have N-terminal extensions with a variable number of O-sulfated tyrosine residues. This modification combined with a number of aspartic and glutamic acid residues results in a highly negatively charged domain of less than 30 amino acids. Osteoadherin (osteomodulin) is a 49,116-Da protein containing 11 leucine-rich repeats (LRRs), 3-4 tyrosine sulfate residues at the N-terminus, and six potential glycosylation sites for N-linked KS Osteoadherin/OSAD/OMD Polyclonal antibody specifically detects Osteoadherin/OSAD/OMD in Human, Mouse, Rat, Porcine, Bovine, Canine, Equine, Guinea Pig, Rabbit, Zebrafish samples. It is validated for Western Blot.