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T2327

Sigma-Aldrich

Trypsin inhibitor

lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)

Sinónimos:

Kunitz Inhibitor

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About This Item

Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.77

product name

Trypsin Inhibitor from Glycine max (soybean), BioUltra, lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)

origen biológico

Glycine max (soybean)

Línea del producto

BioUltra

Análisis

≥95% (Kunitz inhibitor, SDS-PAGE)

formulario

lyophilized powder

temp. de almacenamiento

2-8°C

Descripción general

Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site.

Aplicación

Trypsin Inhibitor from Glycine max (soybean) has been used:
  • as a standard protein to measure the amount of endogenous trypsin inhibitor present in midgut lysate (M1) of Riptortus pedestris
  • as a standard to compare the trypsin inhibitory activity of the purified protein
  • to monitor the trypsin inhibitory activity by fractionating in MonoS cation exchange chromatography
  • as an trypsin inhibitor

Acciones bioquímicas o fisiológicas

Soybean trypsin inhibitor inhibits trypsin and to a lesser extent chymotrypsin and plasmin. It forms a 1:1 stoichiometric complex with trypsin. Upon formation of this complex, trypsin may cleave a single arginine-isoleucine bond in the inhibitor. Dissociation of this complex may yield the modified form or the native inhibitor. At the optimal pH for trypsin binding (pH 8.0), the association constant is ≥ 10x108.
Trypsin Inhibitor from Glycine max (soybean) binds with the active site of trypsin enzyme, in a competitive inhibition manner.

Definición de unidad

One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.

Nota de preparación

Further purification of T9128 yielding an electrophoretically pure Kunitz inhibitor with increased activity.
Trypsin inhibitor is soluble in water and phosphate buffers at concentrations of 10 mg/ml or higher. Solutions at higher concentrations may be hazy and have a yellow to amber color.

Nota de análisis

One mg will inhibit ≥1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.

Otras notas

View more information on Trypsin Inhibitor.

Aplicación

Referencia del producto
Descripción
Precios

Pictogramas

Health hazard

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

Resp. Sens. 1 - Skin Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Functional analysis of the Kunitz trypsin inhibitor family in poplar reveals biochemical diversity and multiplicity in defense against herbivores
Major IT and Constabel CP
Plant Physiology, 146(3), 888-903 (2008)
Xingfei Li et al.
Journal of agricultural and food chemistry, 66(17), 4439-4448 (2018-03-23)
We first observed that protein/polysaccharide interaction exhibited noninteracting behavior which makes Bowman-Birk chymotrypsin inhibitor (BBI) always free of complexation, being separated from another protein with similar isoelectric points, Kunitz trypsin inhibitor (KTI). Turbidity titrations showed that the electrostatic attractions were
A continuous fluorometric assay for trypsin based on melittin and the noncovalent-binding-induced pyrene excimer
Xu N, et al.
Chemistry Letters (Jpn), 42(12), 1528-1530 (2013)
The selective complex behavior between soybean whey proteins and i-carrageenan and isolation of the major proteins of the soybean whey
Li X, et al.
Food Hydrocolloids, 56, 207-217 (2016)
Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks
Arques MC, et al.
Food Chemistry, 155, 24-30 (2014)

Protocolos

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

Chromatograms

application for HPLC

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