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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. 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 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. 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

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Among its related pathways are Diseases of glycosylation and HIV Life Cycle . An important paralog of this gene is KERA. T1 - Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein. AU - Ramstad, VE. AU - Franzén, Ahnders.

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.

It promotes integrin (a vb 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847).

Human Osteoadherin/Osteomodulin ELISA Kit from Invitrogen (96 Tests). 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.

Osteoadherin

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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. 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.
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It promotes integrin (α v β 3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegård, D. (1998) J. Cell Biol. 141, 839–847). Osteoadherin (OSAD) is a bone proteoglycan containing keratan sulfate that belongs to the small leucine-rich proteoglycan (SLRP) family. Osteoadherin promotes Integrin αvβ3-mediated cell binding. The central region of Osteoadherin consists of eleven B-type, leucine-rich repeats ranging in length from 20 to 30 residues.

It had an apparent molecular mass of 85 kD under reducing conditions by SDS-PAGE. 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.
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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 1998-07-03 Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues.


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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.