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MilliporeSigma

B3133

Sigma-Aldrich

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride

trypsin substrate, chromogenic, ≥99% (TLC), powder, suitable for substrate for trypsin

Sinónimos:

L-BAPA, L-BAPNA, BANI

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About This Item

Fórmula empírica (notación de Hill):
C19H22N6O4 · HCl
Número de CAS:
Peso molecular:
434.88
Beilstein/REAXYS Number:
4081878
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride, ≥99% (TLC), suitable for substrate for trypsin

Quality Level

assay

≥99% (TLC)

form

powder

solubility

acetone: water (1:1): 50 mg/mL

suitability

suitable for substrate for trypsin

storage temp.

−20°C

SMILES string

Cl[H].NC(=N)NCCC[C@H](NC(=O)c1ccccc1)C(=O)Nc2ccc(cc2)[N+]([O-])=O

InChI

1S/C19H22N6O4.ClH/c20-19(21)22-12-4-7-16(24-17(26)13-5-2-1-3-6-13)18(27)23-14-8-10-15(11-9-14)25(28)29;/h1-3,5-6,8-11,16H,4,7,12H2,(H,23,27)(H,24,26)(H4,20,21,22);1H/t16-;/m0./s1

InChI key

DEOKFPFLXFNAON-NTISSMGPSA-N

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General description

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride is a substrate for trypsin.

Application

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride has been used as a substrate:
  • for chymotrypsin and trypsin activity assay in enzymatic extract (EE) of M. tenellum and pancreatic tissue homogenates
  • in trypsin and papain standard curve generation
  • in serine protease and fibrinogenolytic assays of eupolytin1 protein

Linkage

Similar to B3279, but produced for Sigma.

Substrates

Chromogenic substrate for trypsin and other proteolytic enzymes.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Enzymatic Assays and Enzyme Histochemistry of Tuta absoluta Feeding on Tomato Leaves
Hamza R, et al.
BMC plant biology, 8(17), 1256-1263 (2018)
Feeding colostrum, its composition and feeding duration variably modify proliferation and morphology of the intestine and digestive enzyme activities of neonatal calves
Blattler U, et al.
The Journal of Nutrition, 131(4), 1256-1263 (2001)
The action of trypsin on synthetic chromogenic arginine substrates
Somorin O, et al.
Journal of Biochemistry, 85(1), 157-162 (1979)
In vitro protein digestibility of animal, vegetal and microbial feed ingredients for Macrobrachium tenellum
Nolasco-Soria H, et al.
Latin American Journal of Aquatic Research, 46(3), 157-162 (2018)
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)

Contenido relacionado

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

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