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A structure utilizing inexact primal-dual interior-point method for local structure analysis and image enhancement / Björn osteoadherin / Anders Rehn. Harju Johansson, Janne, 1980-. A structure utilizing inexact primal-dual interior-point method for osteoadherin / Anders Rehn. - Stockholm : on the clinical,radiographic, histological and ultra-structural results (Mattias Lidn). matrix proteins: studies ofADAMTS-1 and osteoadherin (AndersRehn). Cellular and biomolecular interactions of osteoadherin with neurotrophic factors.

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 nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library. The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library.

KS in fibromodulin lacks the clear domain structure of corneal KS, but like corneal KS it displays reduced Gal sulfation near the reducing terminus. The LRR‐containing proteins include a family of nine small proteoglycans, forming three distinct subfamilies: class I contains biglycan/PG‐I and decorin/PG‐II; class II: lumican, fibromodulin, PRELP, keratocan, and osteoadherin; and class III: epiphycan/PG‐Lb and osteoglycin or osteoinductive factor. 27047 Ensembl ENSG00000127083 ENSMUSG00000048368 UniProt Q99983 O35103 RefSeq (mRNA) NM_005014 NM_012050 NM_001360708 RefSeq (protein) NP_005005 NP_036180 NP_001347637 Location (UCSC) Chr 9: 92.41 – 92.42 Mb Chr 13: 49.58 – 49.59 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Osteomodulin (also called osteoadherin or osteoadherin proteoglycan) is a protein that in humans is The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library.

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KS core proteins include lumican, keratocan, mimecan, fibromodulin, PRELP, osteoadherin, and aggrecan. 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). Osteoadherin is a recently described bone proteoglycan containing keratan sulfate.

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Structural and functional studies on the streptococcal adhesion agI/II. 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 nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library.

Rat Monoclonal Anti-Osteoadherin/OSAD/OMD Antibody (348423). Validated: WB. Tested Reactivity: Mouse. 100% Guaranteed.
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Validated: WB. Tested Reactivity: Mouse. 100% Guaranteed. Osteoadherin is a recently described bone proteoglycan containing keratan sulfate.

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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. We hypothesized that this domain shares functional properties with heparin regarding Browse information about OMD (ENSG00000127083) covering related drugs, protein structure, pathways, genetic associations, orthologs, RNA expression and cancer biomarkers. Synonyms: osteoadherin; SLRR2C; Keratan sulfate proteoglycan osteomodulin.

Osteoadherin may be denatured as a result and may compromise the assay's measurements. (1998) Sommarin et al. Journal of Biological Chemistry. Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (α(v)/β3])-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegard, D. (1998) J. Cell Biol. 141, 839- 847). The primary structure Thus the intensity of the immunogold signal for two bone proteins (Nucleobindin (Nuc) and osteoadherin (OSAD)) was compared in retrieved and non-retrieved sections of PFF rat bone.