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Merck

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:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77

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product name

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

biological source

Glycine max (soybean)

Quality Level

product line

BioUltra

assay

≥95% (Kunitz inhibitor, SDS-PAGE)

form

lyophilized powder

storage temp.

2-8°C

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Este artículo
A4018A9045A9414
gel strength

≥250 g/cm2 (1% gel)

gel strength

≥200 g/cm2 (1% gel)

gel strength

≥200 g/cm2 (1% gel)

gel strength

≥200 g/cm2 (1% gel)

EEO

≤0.12

EEO

≤0.10

EEO

≤0.1

EEO

≤0.10

Quality Level

200

Quality Level

200

Quality Level

-

Quality Level

200

transition temp

gel point 26 °C ±2 °C (1.5% gel)

transition temp

congealing temperature 26-30 °C

transition temp

congealing temperature 26-30 °C

transition temp

congealing temperature 26-30 °C

technique(s)

electrophoresis: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | insect: suitable, cell culture | mammalian: suitable, cell culture | plant: suitable

technique(s)

-

General description

Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site.[1]

Application

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[2]
  • as a standard to compare the trypsin inhibitory activity of the purified protein[3]
  • to monitor the trypsin inhibitory activity by fractionating in MonoS cation exchange chromatography[1]
  • as an trypsin inhibitor[4]

Biochem/physiol Actions

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.[5]

Unit Definition

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.

Preparation Note

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.

Analysis Note

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

Other Notes

View more information on Trypsin Inhibitor.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

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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Visite la Librería de documentos

Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks
Arques MC, et al.
Food Chemistry, 155, 24-30 (2014)
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)
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 midgut lysate of the Riptortus pedestris has antibacterial activity against LPS O-antigen-deficient Burkholderia mutants
Am Jang H, et al.
Developmental and Comparative Immunology, 67, 97-106 (2017)

Protocolos

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

Chromatograms

application for HPLC

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