H6268
Hide–Remazol Brilliant Blue R
protease substrate, powder
Synonym(s):
Hide powder azure, Remazol Brilliant Blue R–Hide
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About This Item
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product name
Hide–Remazol Brilliant Blue R, protease substrate
form
powder
storage temp.
2-8°C
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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
Other Notes
Hide powder covalently linked to Remazol Brilliant Blue R
Substrates
Chromogenic substrate for trypsin
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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)
C Kooi et al.
Journal of bacteriology, 187(13), 4421-4429 (2005-06-22)
Burkholderia cenocepacia ZmpA is expressed as a preproenzyme typical of thermolysin-like proteases such as Pseudomonas aeruginosa LasB and Bacillus thermoproteolyticus thermolysin. The zmpA gene was expressed using the pPRO-EXHTa His(6) tag expression system, which incorporates a six-His tag at the
Boophilus microplus: multiple proteolytic activities in the midgut.
J Mendiola et al.
Experimental parasitology, 82(1), 27-33 (1996-01-01)
T Omori-Satoh et al.
Biochimica et biophysica acta, 1246(1), 61-66 (1995-01-05)
Two hemorrhagic principles (Bitis arietans hemorrhagin a and b: abbreviated as BHRa and BHRb) were purified from the venom of the viperous snake Bitis arietans (puff adder) by gel filtration, ion-exchange and absorption chromatography. A 10-fold purification was achieved for
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