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S1899

Sigma-Aldrich

N-Succinyl-Gly-Gly-Phe-p-Nitroanilid

protease substrate, ≥98% (TLC), powder

Synonym(e):

Suc-Gly-Gly-Phe-PNA

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About This Item

Empirische Formel (Hill-System):
C23H25N5O8
CAS-Nummer:
68982-90-1
Molekulargewicht:
499.47
EG-Nummer:
273-486-7
MDL-Nummer:
MFCD00038721
UNSPSC-Code:
12352204
PubChem Substanz-ID:
24899502
NACRES:
NA.32

product name

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

Assay

≥98% (TLC)

Form

powder

Löslichkeit

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

Lagertemp.

−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)

InChIKey

CFYIUBWVKZQDOG-UHFFFAOYSA-N

Substrate

Substrate for chymotrypsin and for S. griseus protease B.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

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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
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
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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Artikel

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

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