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

Name: N-Succinyl-Gly-Gly-Phe-<I>p</I>-nitroanilide
Brand: SIGMA

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

NACRES:

NA.32

PubChem Substance ID:

24899502

UNSPSC Code:

12352204

EC Number:

273-486-7

MDL number:

MFCD00038721

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Properties

Product Name

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

Quality Level

200

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

Description

General description

Substrate for chymotrypsin and for S. griseus protease B.

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This Item	S2628	G0142	G2901
Sigma-Aldrich S1899 N-Succinyl-Gly-Gly-Phe-p-nitroanilide	Sigma-Aldrich S2628 N-Succinyl-L-phenylalanine-p-nitroanilide	Sigma-Aldrich G0142 Gly-Phe p-nitroanilide	Sigma-Aldrich G2901 Gly-Pro p-nitroanilide p-toluenesulfonate salt
assay ≥98% (TLC)	assay ≥98% (TLC)	assay ≥98% (TLC)	assay ~99% (TLC)
solubility acetic acid: 20 mg/mL, clear, colorless to faintly yellow	solubility dioxane: 25 mg/mL, clear, colorless to faintly yellow	solubility DMF: 50 mg/mL, clear, yellow	solubility 1 M HCl: 50 mg/mL
Quality Level 200	Quality Level 200	Quality Level 200	Quality Level 200
form powder	form powder	form powder	form powder
storage temp. −20°C	storage temp. −20°C	storage temp. −20°C	storage temp. −20°C

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Purification, biochemical and molecular analysis of a chymotrypsin protease with prophenoloxidase suppression activity from the entomopathogenic nematode Steinernema carpocapsae.

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

Noncovalent modification of chymotrypsin surface using an amphiphilic polymer scaffold: implications in modulating protein function.

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)

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Global Trade Item Number

SKU	GTIN
S1899-100MG	04061836915605
S1899-10MG	04061836915728
S1899-50MG	04061832910178

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