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Merck

T0256

Sigma-Aldrich

Trypsin inhibitor from bovine pancreas

Type I-P, essentially salt-free, lyophilized powder

Sinónimos:

BPTI

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About This Item

Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352202

biological source

bovine pancreas

type

Type I-P

form

essentially salt-free, lyophilized powder

mol wt

~6500 Da (single-chain 58-amino acid peptide)

purified by

crystallization

technique(s)

inhibition assay: suitable

solubility

water: 10 g/L

storage temp.

−20°C

Biochem/physiol Actions

A 58-residue protein whose binding to various serine proteases has been extensively studied. It is highly homologous to a family of mamba snake dendrotoxin proteins that inhibit various K+ channels. It also binds to an intracellular site associated with the large conductance Ca2+-activated K+ channel..

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

Prepared by method of Kunitz and Northrup, J. Gen. Physiol., 19, 991 (1936).

Analysis Note

One mg of trypsin inhibitor will inhibit greater than 1.5 mg of trypsin with activity of approximately 10,000 BAEE units per mg protein.
Protein determined by biuret.

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

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

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Fanlu Meng et al.
Journal of plant research, 131(5), 827-837 (2018-05-08)
PeaT1 is a proteinaceous elicitor from fungal pathogen Alternaria tenuissima. Our previous research revealed that this elicitor could induce defense response and enhance disease resistance in various plants including Nicotiana plants. However, immune activation mechanisms whereby PeaT1 elicits defense response
Alexandre P Alloy et al.
The Journal of biological chemistry, 290(35), 21523-21535 (2015-07-16)
Human mesotrypsin is highly homologous to other mammalian trypsins, and yet it is functionally unique in possessing resistance to inhibition by canonical serine protease inhibitors and in cleaving these inhibitors as preferred substrates. Arg-193 and Ser-39 have been identified as
Martina Holubová et al.
The Journal of pharmacology and experimental therapeutics, 366(3), 422-432 (2018-06-20)
Ghrelin, the only known orexigenic gut hormone produced primarily in the stomach, has lately gained attention as a potential treatment of anorexia and cachexia. However, its biologic stability is highly limited; therefore, a number of both peptide and nonpeptide ghrelin
C L Dumke et al.
Journal of applied physiology (Bethesda, Md. : 1985), 92(2), 657-664 (2002-01-18)
Serum proteins [molecular weight (MW) > 10,000] are essential for increased insulin-stimulated glucose transport after in vitro muscle contractions. We investigated the role of the kallikrein-kininogen system, including bradykinin, which is derived from kallikrein (MW > 10,000)-catalyzed degradation of serum
Maurizio Trovato et al.
Biochemical and biophysical research communications, 302(2), 311-315 (2003-02-27)
The design of minimal units required for enzyme inhibition is a major field of interest in structural biology and biotechnology. The successful design of the cyclic dodecapeptide corresponding to the Phe17-Val28 reactive site amino acid sequence of the low-molecular-mass trypsin

Chromatograms

application for HPLC

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