T2327
Trypsin inhibitor
lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)
Synonyme(s) :
Kunitz Inhibitor
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.77
Produits recommandés
product name
Trypsin Inhibitor from Glycine max (soybean), BioUltra, lyophilized powder, ≥95% (Kunitz inhibitor, SDS-PAGE)
Source biologique
Glycine max (soybean)
Gamme de produits
BioUltra
Pureté
≥95% (Kunitz inhibitor, SDS-PAGE)
Forme
lyophilized powder
Température de stockage
2-8°C
Catégories apparentées
Description générale
Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site.
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
- 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
Actions biochimiques/physiologiques
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.
Définition de l'unité
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.
Notes préparatoires
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.
Remarque sur l'analyse
One mg will inhibit ≥1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.
Autres remarques
View more information on Trypsin Inhibitor.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1 - Skin Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
Quantitative determination of active Bowman-Birk isoinhibitors, IBB1 and IBBD2, in commercial soymilks
Arques MC, et al.
Food Chemistry, 155, 24-30 (2014)
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)
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