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Merck

T0256

Sigma-Aldrich

Trypsin-Inhibitor aus Rinderpankreas

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

Synonym(e):

BPTI

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About This Item

CAS-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352202

Biologische Quelle

bovine pancreas

Typ

Type I-P

Form

essentially salt-free, lyophilized powder

Mol-Gew.

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

Aufgereinigt durch

crystallization

Methode(n)

inhibition assay: suitable

Löslichkeit

water: 10 g/L

Lagertemp.

−20°C

Biochem./physiol. Wirkung

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..

Einheitendefinition

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.

Angaben zur Herstellung

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

Hinweis zur Analyse

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.

Sonstige Hinweise

View more information on Trypsin Inhibitor.

Anwendung

Produkt-Nr.
Beschreibung
Preisangaben

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1 - Skin Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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

Verwandter Inhalt

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Chromatograms

application for HPLC

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