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Regulation and function of mineralized tissue extra-cellular matrix proteins : Studies of ADAMTS-1 and osteoadherin. Author: Rehn, Anders. Date: 2008-06-04.

1997-05-01 · Osteoadherin. Short name: OSAD.

This subsection of the Names and taxonomy section indicates the name (s) of the gene (s) that code for the protein sequence (s) described in the entry. Osteoadherin is a recently described bone proteoglycan containing keratan sulfate.

Osteoadherin

Q99983 proteoglycan osteomodulin) ( KSPG Osteoadherin is highly expressed in mineralized tissues, including bone and dentin; however, it's precise roles remain unknown. We investigated the Omd The regulation of osteoadherin by neurotrophins in both osteoblasts and dental tissue extra-cellular matrix proteins : Studies of ADAMTS-1 and osteoadherin. Identification, distribution and expression of osteoadherin during tooth formation. U Petersson, K Hultenby, M Wendel. European journal of oral sciences 111 (2), Osteoadherin is a recently described bone proteoglycan containing keratan sulfate.

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

Utility Header Menu Right. 800-343-7475; Contact Us; Cart We calculate the sensitivity of this ELISA kit by converting cutoff O.D. value, calculated as the average of 20 negative controls plus 2 standard deviations of the 20 negative controls, into a concentration.

OSTEOADHERIN. From THE INSTITUTE OF ODONTOLOGY, CENTER FOR ORAL BIOLOGY Karolinska Institutet, Stockholm, Sweden REGULATION AND FUNCTION OF MINERALIZED TISSUE EXTRA-CELLULAR MATRIX PROTEINS: STUDIES OF ADAMTS-1 AND OSTEOADHERIN Anders Rehn Stockholm 2008 . 2008 Gårdsvägen 4, 169 70 Solna

Our Osteoadherin/OSAD/OMD Antibodies can be used in a variety of model species: Human, Mouse.

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). 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 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). 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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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).

800-343-7475; Contact Us; Cart We calculate the sensitivity of this ELISA kit by converting cutoff O.D. value, calculated as the average of 20 negative controls plus 2 standard deviations of the 20 negative controls, into a concentration.
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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

Sensitivity: 1.4 ng/mL OMD (Osteomodulin) is a Protein Coding gene. Diseases associated with OMD include Bladder Carcinoma In Situ and Anthracosilicosis . Among its related pathways are Diseases of glycosylation and HIV Life Cycle . An important paralog of this gene is KERA.

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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

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.

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).

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. 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.

T1 - Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein. AU - Ramstad, VE. AU - Franzén, Ahnders. AU - Heinegård, Dick. AU - Wendel, M. AU - Reinholt, FP. N1 - The information about affiliations in this record was updated in December 2015. 1999-12-30 · Osteoadherin is a cell binding keratan sulfate proteoglycan which was recently isolated from mineralized bovine bone and subsequently cloned and sequenced.