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Quantitate human OMD in supernatant, serum and plasma. Sensitivity: 1.4 ng/mL 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). Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. Osteoadherin is a recently described bone proteogly-can containing keratan sulfate. It promotes integrin (a vb 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol.

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. 2017-02-28 Osteomodulin (also called osteoadherin or osteoadherin proteoglycan) is a protein that in humans is encoded by the OMD gene. References Further reading. This page was last edited on 12 October 2020, at 04:35 (UTC). Text is available under the Creative Commons Attribution Listed are ELISA Kits for the detection of Osteoadherin, an alias name of osteomodulin. 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.

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.

The Human Osteoadherin IQELISA™ kit is an ultrasensitive ELISA utilizing qPCR detection for 10X more sensitivity with 10X less sample. Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown. The present study determined the Omd expression levels and investigated the effects of over‑ and under‑expression of osteoadherin in osteoblastic cells. Our Osteoadherin/OSAD/OMD Antibodies can be used in a variety of model species: Human, Mouse. Use the list below to choose the Osteoadherin/OSAD/OMD Antibody which is most appropriate for your research; you can click on each one to view full technical details, images, references, reviews and related products. Country/Region selector.

The present study determined the Omd expression levels and investigated the effects of over‑ and under‑expression of osteoadherin in osteoblastic cells. 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.
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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). LRR motifs consist of approximately 2030 amino acids (aa) with conserved leucine spacing, folded into a structure with one βsheet and one 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 For osteoadherin (also called osteomodulin), a cluster of sulfotyrosines is found in the N-terminal region, while two adjacent sulfotyrosine residues are present in the C-terminal region.

Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. Osteoadherin is a recently described bone proteogly-can containing keratan sulfate. It promotes integrin (a vb 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847). The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone 1997-05-01 Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix.
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We hypothesized that this domain shares functional properties with heparin 2000-02-01 Copying, scanning & printing Study spaces & reading rooms Sweden stands up for open access – cancels agreement with Elsevier LUBcat LIBRIS Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (alphav beta3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegârd, D. (1998) J. Cell Biol. 141, 839-847). The primary structure of bovine osteoadherin has now been determined by nucleo … 2019-10-18 · Osteoadherin (also termed osteomodulin) is encoded by the Omd gene and is a keratan sulfate proteoglycan of the class II subfamily of SLRPs. Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown.

Osteoadherin antibody; Osteoadherin proteoglycan antibody; Osteomodulin antibody; SLRR2C antibody.
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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.