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89064

Sigma-Aldrich

4-Phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg trifluoroacetate salt

collagenase substrate, chromogenic, ≥95% (HPLC), powder

Synonym(s):

Pz-Pro-Leu-Gly-Pro-D-Arg trifluoroacetate salt

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About This Item

Empirical Formula (Hill Notation):
C38H52N10O8 · xC2HF3O2
Molecular Weight:
776.88 (free base basis)
UNSPSC Code:
12352204
NACRES:
NA.32
Pricing and availability is not currently available.

Product Name

4-Phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg trifluoroacetate salt, ≥95% (HPLC)

Assay

≥95% (HPLC)

form

powder

Related Categories

Application

4-Phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg trifluoroacetate salt has been used as substrate for collagenase.[1][2]

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
BCCK7681
BCCH4116
BCCF0586
BCCD1051
BCBX1191

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Highly sensitive assay for PZ-peptidase activity by high-performance liquid chromatography
Chikuma, T., et al.
Journal of Chromatography A, 348, 205-212 (1985)
T Chikuma et al.
Journal of chromatography, 635(1), 81-87 (1993-04-09)
A rapid and sensitive assay method for the determination of PZ-peptidase activity is reported. This method is based on the monitoring of the absorption at 320 nm of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu (PZ-Pro-Leu), enzymatically formed from the substrate 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (PZ-peptide), after separation by
M Nagelschmidt et al.
Biochimica et biophysica acta, 571(1), 105-111 (1979-11-09)
A peptidase cleaving a synthetic substrate for collagen peptidases, 4-phenylazobenzyloxcarbonyl-L-Pro-L-Leu-Gly-L-pro-D-Arg (designated as PZ-peptide) has been purified 1200-fold from rabbit serum and characterized. The enzyme preparation is free of collagenase and unspecific proteinase activity. The natural substrates are denatured collagen and
The induction of collagenase and a neutral proteinase by their high molecular weight substrates in Achromobacter iophagus.
V Keil-Dlouha et al.
Journal of molecular biology, 107(3), 293-305 (1976-11-05)
C H Evans
The Biochemical journal, 195(3), 677-684 (1981-06-01)
Tervalent cations of the lanthanide (rare-earth) elements reversibly inhibit bacterial collagenase (clostridiopeptidase A; EC 3.4.24.3). Sm(3+), whose ionic radius is closest to that of Ca(2+), is the most effective inhibitor, completely suppressing clostridiopeptidase activity at a concentration of 100mum in
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