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Trypsin inhibitor from Phaseolus limensis (lima bean), Type II-L, crude powder
biological source
Phaseolus limensis (lima bean)
Quality Level
type
Type II-L
form
crude powder
mol wt
9 kDa
solubility
0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL
storage temp.
2-8°C
General description
Monomer has an apparent molecular weight of approx. 9,000 Da but undergoes a concentration and pH-dependent dimerization.
Application
Trypsin inhibitor from Phaseolus limensis (lima bean) has been used:
- in the inhibition of trypsin in human plasma
- in the termination of proteolytic digestion in rabbit skeletal muscles
- in the inhibition of salivary glands enzyme extract from Lygus lineolaris
- in the inhibition of proteolytic activity in Agave tequilana enzyme extract
Trypsin inhibitor has been used as an affinity ligand for isolation of elastase-type enzymes.
Biochem/physiol Actions
Trypsin inhibitor from lima beans belongs to Bowman-Birk family of protease inhibitors. It is 9 kDa in molecular weight and contains nine disulfide bridges and is highly thermostable. It has trypsin and chymotrypsin binding subdomains.
Preparation Note
Prepared by a modification of the method of Tauber, H., et al., J. Biol. Chem., 179, 1155 (1949) (modified).
Analysis Note
One mg will inhibit ≥0.8 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein.
Other Notes
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.
View more information on Trypsin Inhibitor.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Classe de stockage
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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Protocoles
This technical article described the Enzymatic Assay of Trypsin Inhibitor.
Articles
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
Contenu apparenté
G Bellon et al.
Artery, 7(4), 290-302 (1980-01-01)
A serine protease active on insoluble elastin at neutral pH has been isolated from human aortic media employing a Lima-bean trypsin inhibitor - Sepharose column. It is also hydrolyzed Suc (Ala)3 pna and casein but was found inactive against Benzoyl-Tyr-pna
In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case
Debreczeni J, et al.
Acta crystallographica. Section D, Structural biology, 59(2), 393-395 (2003)
Are cardiovascular and sympathoadrenal effects of human ?new pressor protein? preparations attributable to human coagulation beta-FXIIa?
Papageorgiou PC, et al.
American Journal of Physiology. Heart and Circulatory Physiology, 286(3), H837-H846 (2004)
Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| T9378-500MG | 04061833265888 |
| T9378-100MG | 04061835513277 |
| T9378-1G | 04061826745991 |
