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S1899

Sigma-Aldrich

N-Succinyl-Gly-Gly-Phe-p-nitroanilide

protease substrate, ≥98% (TLC), powder

Synonym(s):

Suc-Gly-Gly-Phe-PNA

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About This Item

Empirical Formula (Hill Notation):
C23H25N5O8
CAS Number:
68982-90-1
Molecular Weight:
499.47
EC Number:
273-486-7
MDL number:
MFCD00038721
UNSPSC Code:
12352204
PubChem Substance ID:
24899502
NACRES:
NA.32

product name

N-Succinyl-Gly-Gly-Phe-p-nitroanilide, protease substrate

Assay

≥98% (TLC)

form

powder

solubility

acetic acid: 20 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

OC(=O)CCC(=O)NCC(=O)NCC(=O)NC(Cc1ccccc1)C(=O)Nc2ccc(cc2)N(=O)=O

InChI

1S/C23H25N5O8/c29-19(10-11-22(32)33)24-13-20(30)25-14-21(31)27-18(12-15-4-2-1-3-5-15)23(34)26-16-6-8-17(9-7-16)28(35)36/h1-9,18H,10-14H2,(H,24,29)(H,25,30)(H,26,34)(H,27,31)(H,32,33)

InChI key

CFYIUBWVKZQDOG-UHFFFAOYSA-N

Substrates

Substrate for chymotrypsin and for S. griseus protease B.

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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Natesan Balasubramanian et al.
International journal for parasitology, 39(9), 975-984 (2009-03-03)
A chymotrypsin serine protease (designated Sc-CHYM) was purified by gel filtration and anion-exchange chromatography from excretory-secretory products of parasitic stage Steinernema carpocapsae. The purified protease had an apparent molecular mass of 30kDa and displayed a pI of 5.9. This protease
Britto S Sandanaraj et al.
Journal of the American Chemical Society, 127(30), 10693-10698 (2005-07-28)
We report here on a new amphiphilic homopolymer that binds noncovalently to proteins. This polymer not only binds to the target protein chymotrypsin with submicromolar affinity but also stabilizes the native structure of the protein. Since the polymer-protein binding process
New proteolytic enzymes in yeast.
T Achstetter et al.
Archives of biochemistry and biophysics, 207(2), 445-454 (1981-04-01)
Ning Luan et al.
Thrombosis and haemostasis, 117(6), 1031-1039 (2017-03-10)
The repugnatorial glands of millipedes release various defensive chemical secretions. Although varieties of such defensive secretions have been studied, none of them is protein or peptide. Herein, a novel factor Xa (FXa) inhibitor named joannsin was identified and characterised from repugnatorial glands
Jorge Frias et al.
Journal of microbiology and biotechnology, 31(2), 327-337 (2020-11-06)
Fibrinolytic enzymes with a direct mechanism of action and safer properties are currently requested for thrombolytic therapy. This paper reports on a new enzyme capable of degrading blood clots directly without impairing blood coagulation. This enzyme is also non-cytotoxic and
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