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Blyscan™ Dye & Dissociation Reagents

  • Regulatory status:RUO
  • Type:Colorimetric assay
  • Other names:Glycosaminoglycan, sGAG
  • Species:Multispecies
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Cat. No. Size Price


B1500 2x 2x 110 ml
PubMed Product Details
Technical Data

Cat # changed from RBCB1500 to B1500

Type

Colorimetric assay

Applications

Cell culture and/or animal studies, Urine, Synovial fluid, Tissue extract

Shipping

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

Storage/Expiration

All components are stable for one year, (from Invoice Date), when stored at 15–25ºC. Do not store below +4ºC. Once opened the glass vial containing sGAG standard should however be stored at +4ºC.

Summary

Features

  • The Blyscan Assay is a quantitative dye-binding method for the analysis of sulfated proteoglycans and glycosaminoglycans, (sGAG).
  • Test material can be assayed directly when present in a soluble form, or following papain extraction from biological materials. The assay can be used to measure the total sGAG content and can also be adopted to determine the O- and N-sulfated glycosaminoglycan ratio within test samples.
  • The dye label used in the assay is 1, 9-dimethylmethylene blue and the dye is employed under conditions that provide a specific label for the sulfated polysaccharide component of proteoglycans or the protein free sulfated glycosaminoglycan chains.
  • The assay is not suitable for small sulfated disaccharide fragments or for samples containing alginates, as these contain uronic acid.
  • Time required is 1 hour.
  • Manufactured by Biocolor.

Research topic

Extracellular matrix, Animal studies

Summary

Glycosaminoglycans (GAGs) are large complex carbohydrate molecules that interact with a wide variety of proteins involved in physiological and pathological processes. GAGs are also known as mucopolysaccharides due to their viscous, lubricating properties, as found in mucous secretions. GAGs are found on all animal cell surfaces in the extracellular matrix (ECM), and some are known to bind and regulate certain proteins, including chemokines, cytokines, growth factors, morphogens, enzymes and adhesion molecules.

GAGs are linear, sulphated, negatively charged polysaccharides that have molecular weights of approximately 10–100 kDa. GAGs can be divided into two main types. Non‐sulphated GAGs include hyaluronic acid (HA), whereas sulphated GAGs include chondroitin sulphate (CS), dermatan sulphate (DS), keratan sulphate (KS), heparin and heparan sulphate (HS).

GAGs play an important role in cell signaling and development, angiogenesis, axonal growth, tumour progression, metastasis and anti‐coagulation. Uncontrolled progenitor cell proliferation leads to malignant tissue transformation and cancer. GAGs and proteoglycans (PGs) are believed to play a critical role in cell proliferation, acting as co‐receptors for growth factors of the fibroblast growth factor (FGF) family.

PGs are composed of a core protein to which one or more GAG chains are covalently attached. Examples of large PGs are aggrecan, the major PG in cartilage, and versican, which is present in numerous adult tissues such as blood vessels and skin. PGs are known to have a variety of functions, dependent on type and in vivo location, and have important roles in invertebrate and vertebrate development, maintenance, and tissue repair. Many biologically potent small proteins can bind GAG chains as a major part of their function in the ECM, at the cell surface, and also in some intracellular locations. Thus, PGs have become a major focus in research on many diseases.

Summary References (12)

References to Glycosaminoglycan

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  • Casu B, Lindahl U. Structure and biological interactions of heparin and heparan sulfate. Adv Carbohydr Chem Biochem. 2001;57:159-206. doi: 10.1016/s0065-2318(01)57017-1. PMID: 11836942. See more on PubMed
  • Couchman JR, Pataki CA. An introduction to proteoglycans and their localization. J Histochem Cytochem. 2012 Dec;60(12):885-97. doi: 10.1369/0022155412464638. Epub 2012 Sep 26. PMID: 23019015; PMCID: PMC3527888. See more on PubMed
  • Gandhi NS, Mancera RL. The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des. 2008 Dec;72(6):455-82. doi: 10.1111/j.1747-0285.2008.00741.x. PMID: 19090915. See more on PubMed
  • Holt CE, Dickson BJ. Sugar codes for axons? Neuron. 2005 Apr 21;46(2):169-72. doi: 10.1016/j.neuron.2005.03.021. PMID: 15848796; PMCID: PMC3687205. See more on PubMed
  • Iozzo RV, San Antonio JD. Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena. J Clin Invest. 2001 Aug;108(3):349-55. doi: 10.1172/JCI13738. PMID: 11489925; PMCID: PMC209371. See more on PubMed
  • Jackson RL, Busch SJ, Cardin AD. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol Rev. 1991 Apr;71(2):481-539. doi: 10.1152/physrev.1991.71.2.481. PMID: 2006221. See more on PubMed
  • Liu D, Shriver Z, Qi Y, Venkataraman G, Sasisekharan R. Dynamic regulation of tumor growth and metastasis by heparan sulfate glycosaminoglycans. Semin Thromb Hemost. 2002 Feb;28(1):67-78. doi: 10.1055/s-2002-20565. PMID: 11885027. See more on PubMed
  • Sanderson RD. Heparan sulfate proteoglycans in invasion and metastasis. Semin Cell Dev Biol. 2001 Apr;12(2):89-98. doi: 10.1006/scdb.2000.0241. PMID: 11292374. See more on PubMed
  • Sasisekharan R, Shriver Z, Venkataraman G, Narayanasami U. Roles of heparan- sulphate glycosaminoglycans in cancer. Nat Rev Cancer. 2002 Jul;2(7):521-8. doi: 10.1038/nrc842. PMID: 12094238. See more on PubMed
  • Tímár J, Lapis K, Dudás J, Sebestyén A, Kopper L, Kovalszky I. Proteoglycans and tumor progression: Janus-faced molecules with contradictory functions in cancer. Semin Cancer Biol. 2002 Jun;12(3):173-86. doi: 10.1016/S1044-579X(02)00021-4. PMID: 12083848. See more on PubMed
  • Yip GW, Smollich M, Götte M. Therapeutic value of glycosaminoglycans in cancer. Mol Cancer Ther. 2006 Sep;5(9):2139-48. doi: 10.1158/1535-7163.MCT-06-0082. PMID: 16985046. See more on PubMed
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