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C3788

Sigma-Aldrich

Chondroitin sulfate B sodium salt

from Porcine intestinal mucosa, ≥90%, lyophilized powder

Sinónimos:

β-Heparin, Dermatan sulfate sodium salt

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About This Item

Número de CAS:
54328-33-5
MDL number:
MFCD00151683
UNSPSC Code:
12352201
NACRES:
NA.25

biological source

Porcine intestinal mucosa

Quality Level

200

assay

≥90%

form

lyophilized powder

impurities

≤20% water (Karl Fischer)

color

white

solubility

H2O: 5 mg/mL, clear, colorless

cation traces

Na: 7.0-11.5%

storage temp.

2-8°C

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General description

Chondroitin, a glucosaminoglycan (GAG), is a polysaccharide chain of alternating units of N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcA) that can be sulfated on the either or both GalNAc and GlcA units. Chondroitin and its sulfates are frequently attached to proteins to form proteoglycans. Chondroitin sulfate B (Dermatam sulfate) is a component of proteoglycans such as decorin, biglycan and versican. Chondroitin sulfate B is used to study β peptide (1-42) cytotoxicity.

Application

Chondroitin sulfate B may be used to study its roles as a biomolecule receptor, mediator of cell signaling and cell binding molecule. It may be used to compare its properties to those of chondroitin sulfate A and chondroitin sulfate C. Chondroitin sulfate B is used to study β peptide(1-42) cytotoxicity.

Biochem/physiol Actions

As a large, negatively charged, hydrophilic molecule that is too inflexible to fold into a compact globular structure, chondroitin sulfate molecules form porous hydrated gels, providing mechanical support to tissue and allowing rapid diffusion of water-soluble molecules and migration of cells.

Components

Chondroitin Sulfate B is an acidic mucopolysaccharide found in cartilage, skin, cornea, and umbilical cord. It is composed of alternating N-acetylgalactosamine, L-iduronic acid, and sulfate residues in equimolar quantities where carbon 4 of the N-acetylgalactosamines is sulfated.

Caution

Store this product at 2-8°C.

Preparation Note

This product is soluble in water at 100 mg/mL.

Other Notes

To gain a comprehensive understanding of our extensive range of Polysaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Sylvia Gruber et al.
International journal of molecular sciences, 19(6) (2018-06-09)
Oral mucositis is the most frequently occurring early side effect of head-and-neck cancer radiotherapy. Systemic dermatan sulfate (DS) treatment revealed a significant radioprotective potential in a preclinical model of oral mucositis. This study was initiated to elucidate the mechanistic effects
Rebecca Morgan et al.
The Journal of rheumatology, 31(8), 1497-1505 (2004-08-04)
Pristane induced arthritis (PIA) is a seropositive experimental murine model that closely resembles rheumatoid arthritis (RA). Immune reactivity to a broad spectrum of autoantigens has been recognized in this disease model. We investigated the specificity of the autoimmune response in
Sylvia Gruber et al.
Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al], 194(7), 675-685 (2018-03-03)
Oral mucositis is a frequent, dose-limiting side effect of radio(chemo)therapy of head-and-neck malignancies. The epithelial radiation response is based on multiple tissue changes, which could offer targets for a biologically tailored treatment. The potential of dermatan sulfate (DS) to modulate radiation-induced oral
Ana M Saraiva et al.
Macromolecular bioscience, 10(10), 1152-1163 (2010-05-19)
The amyloid-β peptide (Aβ) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. Aβ amyloid formation and deposition are due to a conformational switching to a β-enriched
Ramona Bravo et al.
The Journal of biological chemistry, 283(47), 32471-32483 (2008-09-30)
The histopathological hallmarks of Alzheimer disease are the self-aggregation of the amyloid beta peptide (Abeta) in extracellular amyloid fibrils and the formation of intraneuronal Tau filaments, but a convincing mechanism connecting both processes has yet to be provided. Here we
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