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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

product name

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

Assay

≥95% (HPLC)

form

powder

Application

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

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Collagenase H Is Crucial for Isolation of Rat Pancreatic Islets
Atsushi Fujio
Cell Transplantation (2014)
U Tisljar
Biological chemistry Hoppe-Seyler, 374(2), 91-100 (1993-02-01)
Thimet oligopeptidase (EC 3.4.24.15) is a thiol-dependent metallo-endopeptidase also known as Pz-peptidase, collagenase-like peptidase, endooligopeptidase A, soluble metallo-endopeptidase and endopeptidase 24.15. The enzyme is closely related to the yeast proteinase yscD. Thimet oligopeptidase (M(r) 74000) is widely distributed in animals
A Study of the Collagen-binding Domain of a 116-kDaClostridium histolyticum Collagenase*
Osamu Matsushita
The Journal of Biological Chemistry (1998)
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
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