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Manufactured by BioVendor

Decorin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B
  • Species:Human
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Cat. No. Size Price


RD172324100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 339 AA. MW: 37.6 kDa (calculated). UniProtKB acc.no. P07585 (Asp31-Lys359). N-terminal His-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

MKHHHHHHASDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK

Source

E. coli

Purity

Purity as determined by densitometric image analysis: > 90 %

SDS-PAGE Gel

14% SDS-PAGE separation of Hu Decorin:
1. M.W. marker – 97, 66, 45, 31, 21, 14 kDa
2. reduced and heated sample, 2.5μg/lane
3. non-reduced and non-heated sample, 2.5μg/lane

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized in 0.5 mg/mL in 0.03M Acetate buffer pH 4.0

Reconstitution

Add 0.1 M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/mL. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

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.

Summary References (13)

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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