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Merck

T0256

Sigma-Aldrich

Trypsin inhibitor from bovine pancreas

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

Synonim(y):

BPTI

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About This Item

Numer CAS:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352202

pochodzenie biologiczne

bovine pancreas

typ

Type I-P

Postać

essentially salt-free, lyophilized powder

masa cząsteczkowa

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

oczyszczone przez

crystallization

metody

inhibition assay: suitable

rozpuszczalność

water: 10 g/L

temp. przechowywania

−20°C

Działania biochem./fizjol.

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..

Definicja jednostki

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.

Uwaga dotycząca przygotowania

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

Komentarz do analizy

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.

Inne uwagi

View more information on Trypsin Inhibitor.
This page may contain text that has been machine translated.

Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1 - Skin Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
J N Whitaker et al.
The Biochemical journal, 201(3), 543-553 (1982-03-01)
Previous studies have demonstrated that the kidney is the major site for clearance and catabolism of a peptide (residues 43-88) of encephalitogenic or basic protein (BP) derived from central-nervous-system myelin. In the present investigation rat renal tissue was shown to
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
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

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