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Calcofluor Fluorescent Stain

Calcofluor Fluorescent Stain C-CLFR
Product code: C-CLFR-5G



5 g

Prices exclude VAT

This product has been discontinued

Content: 5 g or 10 g
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Solid
Stability: > 5 years under recommended storage conditions
CAS Number: 4404-43-7
Molecular Formula: C40H44N12O10S2
Molecular Weight: 917.0
Purity: Not Applicable
Method recognition: EBC Method 3.10.2, EBC Method 4.16.2, EBC Method 8.13.2, EBC Method 8.13.3, EBC Method 9.31.2 and ASBC Method Wort 18

These products have been discontinued (read more).

High purity Calcofluor Fluorescent Stain for use in the measurement of 1,3-1,4-β-glucan in wort and beer.

View all available cofactors and stains.

Data booklets for each pack size are located in the Documents tab.


Valorization of native soluble and insoluble oat side streams for stable suspensions and emulsions.

Valoppi, F., Wang, Y. J., Alt, G., Peltonen, L. J. & Mikkonen, K. S. (2021). Food and Bioprocess Technology, 1-14.

Among different cereals, oat is becoming more popular due to its unique composition and health benefits. The increase in oat production is associated with an increase in related side streams, comprising unutilized biomass that is rich in valuable components, such as polysaccharides, proteins, and antioxidants. To valorize such biomass, it is fundamental that side streams enter back into the food production chain, in respect of the circular economy model. Here, we propose the use of soluble and insoluble oat-production side-stream in suspensions and emulsions, avoiding any further extraction, fractionation, and/or chemical derivatization. Our approach further increases the value of these side streams. To this aim, we first studied the effect of thermal and mechanical processes on the behavior and properties of both soluble and insoluble oat side-stream fractions in water and at air/water interface. Then, we characterized the emulsifying and stabilizing abilities of these materials in oil-in-water emulsions. Interestingly, we found that the insoluble fraction was able to form stable suspensions and emulsions after mechanical treatment. The oil droplets in the emulsions were stabilized by anchoring at the surface of the insoluble particles. On the other hand, the soluble fraction formed only stable viscous solutions. Finally, we demonstrated that the two fractions can be combined to increase the storage stability of the resulting emulsion. Our results highlight that oat production side streams can be used as novel bio-based emulsifiers, showing the great potential behind the underutilized cereal-side-stream biomass.

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Cycloheximide-induced phenolic burst in roots of Pisum sativum L.

Tarchevsky, I. A., Ageeva, M. V., Petrova, N. V., Akulov, A. N. & Egorova, A. M. (2017). Applied Biochemistry and Microbiology, 53(5), 568-572.

Chromatography and histochemical analysis of soluble phenolic compounds demonstrated their higher content in the roots of cycloheximide-treated pea plants. These substances accumulated together with lignin in the endodermis and xylem cells of conducting bundles. This finding confirms the antipathogenic cycloheximide effect based on the previous results of proteome analysis.

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Hemoglobin is an effective inducer of hyphal differentiation in Candida albicans.

Pendrak, M. L. & Roberts, D. D. (2007). Medical Mycology, 45(1), 61-71.

Hemoglobin is an abundant protein in the host vascular compartment and a source of iron, heme, and amino acids for many pathogens. The human fungal pathogen Candida albicans uses hemoglobin as an iron source as well as a signaling molecule to alter gene expression and induce adhesion to several extracellular matrix proteins. We now report that hemoglobin can promote true hyphal morphogenesis. Hemoglobin added to yeast cells at 37°C rapidly induced expression of the hypha-specific genes HWP1 and ECE1 coincident with the pattern of hyphal development. A synthetic medium buffered with phosphate at pH 7.2 and containing physiological glucose (5 mM) and low ammonium ion (0.1 mM) was optimal for the response to hemoglobin. High glucose (110 mM), high ammonium ion (20 mM), and 0.1 mM glutamine were all inhibitory. Heme, free globin, or immobilized hemoglobin could not replicate the activity of hemoglobin to induce germ tubes or hypha-specific gene expression at 37°C under optimized conditions. This implicates the previously described Hb-signaling receptor in hyphal formation. This response was also dependent upon the presence of the morphogenesis regulator Efg1p, but the MAP-kinase specific transcription factor Cph1p was not required. These data define a role for the host-factor hemoglobin in Efg1p-dependent hyphal development.

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Safety Data Sheet
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