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H2508

Sigma-Aldrich

Hippuryl-Arg

carboxypeptidase substrate, chromogenic, ≥98% (TLC), powder

Synonym(s):

N-Benzoyl-Gly-Arg

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100 MG
1 390,00 kr
250 MG
3 200,00 kr
500 MG
5 430,00 kr
1 G
10 010,00 kr

1 390,00 kr

Please contact Customer Service for Availability
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100 MG
1 390,00 kr
250 MG
3 200,00 kr
500 MG
5 430,00 kr
1 G
10 010,00 kr

About This Item

Empirical Formula (Hill Notation):
C15H21N5O4
CAS Number:
744-46-7
Molecular Weight:
335.36
EC Number:
212-015-1
MDL number:
MFCD00055706
UNSPSC Code:
12352204
PubChem Substance ID:
24895502
NACRES:
NA.32

1 390,00 kr

Please contact Customer Service for Availability

Product Name

Hippuryl-Arg, carboxypeptidase substrate

Quality Level

200

Assay

≥98% (TLC)

form

powder

solubility

water: 50 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

NC(=N)NCCC[C@H](NC(=O)CNC(=O)c1ccccc1)C(O)=O

InChI

1S/C15H21N5O4/c16-15(17)18-8-4-7-11(14(23)24)20-12(21)9-19-13(22)10-5-2-1-3-6-10/h1-3,5-6,11H,4,7-9H2,(H,19,22)(H,20,21)(H,23,24)(H4,16,17,18)/t11-/m0/s1

InChI key

GFLCPYUSPYXNBV-NSHDSACASA-N

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Application

Hippuryl-Arg has been used as a substrate for:
  • aminopeptidase from Trogoderma granarium[1]
  • exopeptidase from Bactrocera oleae Gmelin,[2] midgut of Plagiodera versicolora[3]
  • carboxypeptidase from Pichia pastoris[4]

Biochem/physiol Actions

Hippuryl-Arg is a synthetic substrate for carboxypeptidase B,[4] and aminopeptidase.[1] The enzyme carboxypeptidase acts on C terminal of arginine and lysine.[4]

Substrates

Substrate for carboxypeptidase B and carboxypeptidase N.

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

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Certificates of Analysis (COA)

Lot/Batch Number
BCCL7778
BCCJ8396
BCCG6942
BCCD2038
BCBX8752

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S Appelros et al.
Biological chemistry, 379(7), 893-898 (1998-08-15)
Recent developments in the treatment of acute pancreatitis have focused on the importance of early determination of the severity of an attack. Measuring levels of activation peptides from pancreatic proenzymes seems to be one way to predict severity. Levels of
Yu-Hong Liu et al.
FEBS letters, 580(22), 5137-5142 (2006-09-12)
This work reports the use of electrospray mass spectrometry for studying the conformational dynamics of enzymes by amide hydrogen/deuterium exchange (HDX) measurements. A rapid-mixing quench-flow approach allows comparisons to be made between the HDX kinetics of free enzymes with those
Digestion and protein metabolism of Trogoderma granarium (Coleoptera: Dermestidae) fed on different barley varieties
Mardani-Talaee M, et al.
Journal of Stored Products Research, 73, 37-41 (2017)
H Schweisfurth et al.
Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie, 21(10), 605-609 (1983-10-01)
Kininase I (carboxypeptidase N; EC 3.4.17.3) consists of carboxypeptidase N1 (CN1) and carboxypeptidase N2 (CN2); these two enzymes can be differentiated by their activities towards hippuryl-L-arginine and hippuryl-L-lysine, respectively. A spectrophotometric assay for both carboxypeptidases in human serum is described
Hidefumi Komura et al.
Microbiology and immunology, 46(2), 115-117 (2002-04-10)
Carboxypeptidases (CP) in plasma and sera serve as regulators of anaphylatoxins such as C3a and C5a. The activity of CP can be measured by determining hippuric acid after cleavage of the small synthetic substrate hippuryl-L-arginine. Although a colorimetric assay is
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