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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
Beilstein/REAXYS Number:
5629635
MDL number:
Product Name
Hide–Remazol Brilliant Blue R, protease substrate
form
powder
storage temp.
2-8°C
Quality Level
General description
Chromogenic substrate for trypsin
Application
Hide−Remazol Brilliant Blue R has been used:
- to study the substrate specificity of a purified collagenase preparation from Clostridium histolyticum
- to mix with cytotoxic samples for hide powder azure protease activity assay
- as a high molecular weight substrate to test the inhibition of trypsin by the purified recombinant rat bikunin, α1-m/bikunin precursor, and α1-m
- as a substrate to obtain the inhibition of snake venom protease activity by the addition of exogenous citrate
Other Notes
Hide powder covalently linked to Remazol Brilliant Blue R
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Citrate inhibition of snake venom proteases
Odell G V, et al.
Toxicon, 36(12), 1801-1806 (1998)
Expression of a functional proteinase inhibitor capable of accepting xylose: bikunin
Falkenberg C, et al.
Archives of Biochemistry and Biophysics, 387(1), 99-106 (2001)
Soluble, dye-labelled substrates for a micro-plate assay of proteinase activity
Wolf G A and Wirth S J
Journal of Microbiological Methods, 25(3), 337-342 (1996)
J Melrose et al.
Archives of orthopaedic and trauma surgery, 114(3), 145-152 (1995-01-01)
Chemonucleolysis is a therapeutic procedure whereby a degradative enzyme is injected intradiscally to reduce disc height/width by depolymerisation of extracellular matrix components. This process is considered to diminish disc pressure on inflamed nerve roots, resulting in the alleviation of sciatic
S Mischke
Microbios, 87(352), 175-183 (1996-01-01)
Four chromogenic substrates were compared, and methods were developed for measuring protease activity from fungi. Digestion of azoalbumin, a water-soluble substrate, resulted in dye release most closely proportional to enzyme activity. Substrates insoluble in water were advantageous for time-course studies
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