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T6140

Sigma-Aldrich

N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt

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

Synonym(s):

N-Tosylglycyl-L-prolyl-L-lysine 4-nitroanilide acetate salt

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About This Item

Linear Formula:
C26H34N6O7S · C2H4O2
CAS Number:
Molecular Weight:
634.70
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt, plasmin substrate

Quality Level

Assay

≥98% (TLC)

form

powder

solubility

ethanol: 50 mg/mL, colorless to yellow

storage temp.

−20°C

SMILES string

CC(O)=O.Cc1ccc(cc1)S(=O)(=O)NCC(=O)N2CCC[C@H]2C(=O)N[C@@H](CCCCN)C(=O)Nc3ccc(cc3)[N+]([O-])=O

InChI

1S/C26H34N6O7S.C2H4O2/c1-18-7-13-21(14-8-18)40(38,39)28-17-24(33)31-16-4-6-23(31)26(35)30-22(5-2-3-15-27)25(34)29-19-9-11-20(12-10-19)32(36)37;1-2(3)4/h7-14,22-23,28H,2-6,15-17,27H2,1H3,(H,29,34)(H,30,35);1H3,(H,3,4)/t22-,23-;/m0./s1

InChI key

KPGSNEYSJPIZCW-SJEIDVEUSA-N

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Application

N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt has been used:
  • as a substrate for examining the amidolytic activity of aprE2, aprE5-41
  • as a substrate for serine protease and fibrinogenolytic assays
  • as a substrate for plasmin assay

Biochem/physiol Actions

N-(p-Tosyl)-Gly-Pro-Lys 4-nitroanilide acetate salt is a chromogenic substrate for plasmin assay, serine protease enzyme activity and fibrinogenolytic assays.

Substrates

A chromogenic substrate for plasmin.

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)

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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Min Wang et al.
International journal of biological macromolecules, 146, 781-789 (2019-11-16)
The heterologous nature of SAK, a thrombolytic drug, elicits high titers of neutralizing antibodies, which limits its clinical use. Here, we aim to establish a SAK mutant with equivalent activity to the wild type but reduced antigenicity, which may allow
Overexpression of aprE2, a Fibrinolytic Enzyme Gene from Bacillus subtilis CH3-5, in Escherichia coli and the Properties of AprE2.
Jeong SJ, et al.
Journal of microbiology and biotechnology, 24(7), 969-978 (2014)
Streptococcus pneumoniae choline-binding protein E interaction with plasminogen/plasmin stimulates migration across the extracellular matrix.
Attali C, et al.
Infection and Immunity, 76(2), 466-476 (2008)
A bi-functional anti-thrombosis protein containing both direct-acting fibrin (ogen) olytic and plasminogen-activating activities
Yang H, et al.
PLoS ONE, 6(3), e17519-e17519 (2011)
Purification and characterization of a major fibrinolytic enzyme from Bacillus amyloliquefaciens MJ5-41 isolated from Meju
Jo HD, et al.
Journal of microbiology and biotechnology, 21(11), 1166-1173 (2011)

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