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N8010

Sigma-Aldrich

4-Nitrophenyl 4-guanidinobenzoate hydrochloride

protease substrate, ≥95.0% (TLC), powder

Synonym(s):

4-Guanidinobenzoic acid 4-nitrophenylester hydrochloride, NPGB, pNPGB

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About This Item

Empirical Formula (Hill Notation):
C14H12N4O4 · HCl
CAS Number:
19135-17-2
Molecular Weight:
336.73
Beilstein:
8024554
EC Number:
242-831-3
MDL number:
MFCD00037010
UNSPSC Code:
12352204
PubChem Substance ID:
24897847
NACRES:
NA.32

product name

4-Nitrophenyl 4-guanidinobenzoate hydrochloride, protease inhibitor and substrate

Quality Level

200

Assay

≥95.0% (TLC)

form

powder

solubility

formic acid: soluble 49.00-51.00 mg/mL

storage temp.

−20°C

SMILES string

Cl[H].NC(=N)Nc1ccc(cc1)C(=O)Oc2ccc(cc2)[N+]([O-])=O

InChI

1S/C14H12N4O4.ClH/c15-14(16)17-10-3-1-9(2-4-10)13(19)22-12-7-5-11(6-8-12)18(20)21;/h1-8H,(H4,15,16,17);1H

InChI key

PKSBDZOBYIKNGY-UHFFFAOYSA-N

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General description

4-Nitrophenyl 4-guanidinobenzoate hydrochloride (pNPGB) is a trypsin substrate. It is more water-soluble than 4-methylumbelliferyl 4-guanidinobenzoate and is preferred in spectrophotometric assay.

Application

4-Nitrophenyl 4-guanidinobenzoate hydrochloride has been used:
  • as a substrate for trypsin for active site titration experiments
  • for pre-treating of mosquito eggs in the interplasmid transposition assay
  • as a component of isotonic buffer to moisten filter paper for mosquito embryo collection

Biochem/physiol Actions

4-Nitrophenyl 4-guanidinobenzoate hydrochloride (pNPGB) inhibits phenoloxidase enzyme and delays embryo chorionic membrane hardening.

Pictograms

Corrosion
GHS05

Signal Word

Danger

Hazard Statements

H318

Precautionary Statements

P280 - P305 + P351 + P338

Hazard Classifications

Eye Dam. 1

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

N8010-BULK:
N8010-500MG-PW:
N8010-1G:
N8010-5G:
N8010-VAR:
N8010-500MG:
N8010-100MG:
N8010-1G-PW:

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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Studies on the Molecular Mechanism of Mersalyl and 4-Aminophenylmercuric Acetate Re-activation of Trypsin-Thiol Complexes
STEVEN FS and GRIFFIN MM
European Journal of Biochemistry, 109(2), 567-573 (1980)
Mekdes Debela et al.
Scientific reports, 8(1), 10705-10705 (2018-07-18)
Human KLK8/neuropsin, a kallikrein-related serine peptidase, is mostly expressed in skin and the hippocampus regions of the brain, where it regulates memory formation by synaptic remodeling. Substrate profiles of recombinant KLK8 were analyzed with positional scanning using fluorogenic tetrapeptides and
J E Dravland et al.
The Journal of experimental zoology, 232(1), 117-128 (1984-10-01)
Previous studies from this laboratory have suggested a role for sperm trypsinlike activity in the membrane events of the hamster sperm acrosome reaction, but these conclusions have been disputed by studies done with guinea pig, mouse, and ram sperm. This
D Collen et al.
The Journal of biological chemistry, 268(11), 8284-8289 (1993-04-15)
The mechanism of activation of human plasminogen by recombinant staphylokinase (STAR) was studied using the active site titrant p-nitrophenyl-p'-guanidinobenzoate (NPGB). NPGB prevented active site exposure in equimolar mixtures of plasminogen and STAR but reacted stoichiometrically with mixtures preincubated in the
S P Leytus et al.
Biochimica et biophysica acta, 788(1), 74-86 (1984-07-17)
A theory and experimental method are presented to characterize the kinetics of fast-acting, irreversible proteinase inhibitors. The theory is based upon formal analysis of the case of an irreversible inhibitor competing with a substrate for the active-site of a proteinase.
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