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Manufactured by BioVendor

Decorin Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B
  • Species:Human
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Cat. No. Size Price


RD193324200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate

Sample Requirements

20 µl/well

Storage/Expiration

Store the complete kit at 2 8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

0.125 – 4 ng/ml

Limit of Detection

56 pg/ml

Intra-assay (Within-Run)

n = 8; CV = 4.0 ng/ml

Inter-assay (Run-to-Run)

n = 6; CV = 5.8 ng/ml

Spiking Recovery

99.0 %

Dilutation Linearity

103.3 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3.5 hours
  • The kit measures decorin in serum, plasma (EDTA, citrate, heparin)
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Cardiovascular disease, Energy metabolism and body weight regulation, Oncology

Summary

Decorin (DCN) belongs to the small leucine-rich proteoglycan (SLRP) family. Decorin is member of the class 1 of SLRP family with relative molecular mass of core protein of 40 kDa and with an attached glycosaminoglycan chain consisting of either chondroitin sulfate (CS) or dermatan sulfate (DS) in the range of 120 to 180 kDa. It has a four-domain structure and domain II contains glycosaminoglycan attachment site and domain III contains 10 leucine-rich repeats (LRR) which are involved in protein-protein interaction.
Decorin is secreted mainly by mesenchymal cells and plays a key role in the regulation of extracellular matrix assembly by binding to several components. Decorin has a high affinity binding site for collagen at LRRs 4-6 and after interaction with collagen affects fibril formation and stabilizes them. These effects may explain the phenotype of decorin null mice characterized by abnormal skin fragility and loosely packed collagen fibers. Binding of decorin with fibronectin and thrombospondin modulates cell adhesion and migration.
In addition, decorin has multiple non-structural functions and interacts with a number of biological molecules such as growth factors (TGF-β, FGF-2, IGF-1, TNF-α), the complement component C1q and epidermal growth factor receptor (EGFR). These interactions are consistent with decorin´s involvement in diverse processes such as tumor growth and metastasis, angiogenesis, renal and pulmonary fibrosis, muscular dystrophy, wound healing and myocardial infarction. Decorin has been shown to have anti-tumorigenic properties in an experimental murine tumor model and is capable of suppressing the growth of various tumor cell lines. Decorin expression in adipose tissue is markedly upregulated in the obese state and may therefore play a role in adipose tissue homeostasis or in pathophysiology associated with obesity and type 2 diabetes. There is evidence from in vitro and in vivo animal models as well as humans to suggest an important role of decorin in attenuating progression of atherosclerosis. Decorin distribution in different blood vessels has been shown to inversely correlate with the tendency to develop atherosclerosis. A recent study described that plasma decorin levels are decreased in patients with acute ischemic stroke and this decorin reduction may be associated with increased risk for ischemic stroke. Other findings indicate that the estrogen-independent anti-proliferative effects of decorin on endometriotic epithelial cells and endometrial stromal cells may contribute to the effectiveness against endometriosis.

References to Summary

References to Decorin

  • Baghy K, Iozzo RV, Kovalszky I. Decorin-TGFbeta axis in hepatic fibrosis and cirrhosis. J Histochem Cytochem. 2012 Apr;60 (4):262-8
  • Bolton K, Segal D, McMillan J, Jowett J, Heilbronn L, Abberton K, Zimmet P, Chisholm D, Collier G, Walder K. Decorin is a secreted protein associated with obesity and type 2 diabetes. Int J Obes (Lond). 2008 Jul;32 (7):1113-21
  • Chen S, Birk DE. Focus on molecules: decorin. Exp Eye Res. 2011 Jun;92 (6):444-5
  • Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol. 1997 Feb 10;136 (3):729-43
  • Guidetti G, Bertoni A, Viola M, Tira E, Balduini C, Torti M. The small proteoglycan decorin supports adhesion and activation of human platelets. Blood. 2002 Sep 1;100 (5):1707-14
  • Hu Y, Sun H, Owens RT, Wu J, Chen YQ, Berquin IM, Perry D, O'Flaherty JT, Edwards IJ. Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways. Neoplasia. 2009 Oct;11 (10):1042-53
  • Iozzo RV. The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. J Biol Chem. 1999 Jul 2;274 (27):18843-6
  • Li Y, Liu Y, Xia W, Lei D, Voorhees JJ, Fisher GJ. Age-dependent alterations of decorin glycosaminoglycans in human skin. Sci Rep. 2013;3:2422
  • Moscatello DK, Santra M, Mann DM, McQuillan DJ, Wong AJ, Iozzo RV. Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor. J Clin Invest. 1998 Jan 15;101 (2):406-12
  • Ono YJ, Terai Y, Tanabe A, Hayashi A, Hayashi M, Yamashita Y, Kyo S, Ohmichi M. Decorin induced by progesterone plays a crucial role in suppressing endometriosis. J Endocrinol. 2014 Nov;223 (2):203-16
  • Singla S, Hu C, Mizeracki A, Mehta JL. Decorin in atherosclerosis. Ther Adv Cardiovasc Dis. 2011 Dec;5 (6):305-14
  • Stokes MB, Holler S, Cui Y, Hudkins KL, Eitner F, Fogo A, Alpers CE. Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease. Kidney Int. 2000 Feb;57 (2):487-98
  • Xu YZ, Zhao KJ, Yang ZG, Zhang YH, Zhang YW, Hong B, Liu JM. Decreased plasma decorin levels following acute ischemic stroke: correlation with MMP-2 and differential expression in TOAST subtypes. Mol Med Rep. 2012 Dec;6 (6):1319-24
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