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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
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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
General description
Chromogenic substrate for trypsin
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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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)
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)
Citrate inhibition of snake venom proteases
Odell G V, et al.
Toxicon, 36(12), 1801-1806 (1998)
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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