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Merck
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T7659

Sigma-Aldrich

Trypsin Inhibitor, Defined (1X) Solution

Animal component free, BioReagent, suitable for cell culture

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About This Item

Número de CAS:
9035-81-8
Número MDL:
MFCD00082102
Código UNSPSC:
12352204
NACRES:
NA.75
En este momento no podemos mostrarle ni los precios ni la disponibilidad

Nivel de calidad

400

esterilidad

sterile-filtered

Línea del producto

BioReagent

Formulario

solution

técnicas

cell culture | mammalian: suitable

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

Aplicación

This product designed to be used during the subculture of keratinocytes contains Kunitz-type soybean trypsin inhibitor (SBTI) which inhibits the catalytic activity of serine proteases such as trypsin and tryptase. It is used in cell culture to stop the action of trypsin which is used to release cells from substratum during passaging. It may be also useful in other anti-serine protease studies.
Used to neutralize the effects of trypsin/EDTA solution.

Forma física

Solution in 98.7% DPBS and 1.3% Soybean Trypsin Inhibitor.

Reconstitución

Use at a minimum volume ratio of 1:1 TID:trypsin/EDTA.

Pictogramas

Health hazard
GHS08

Palabra de señalización

Danger

Frases de peligro

H317,H334

Clasificaciones de peligro

Resp. Sens. 1 - Skin Sens. 1

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificados de análisis (COA)

Lot/Batch Number
RNBL9052
RNBL0682
RNBK6940
RNBJ6151
RNBH8774

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Sarra Djemil et al.
Cellular and molecular neurobiology, 41(8), 1787-1799 (2020-08-30)
Septal innervation of basal forebrain cholinergic neurons to the hippocampus is critical for normal learning and memory and is severely degenerated in Alzheimer's disease. To understand the molecular events underlying physiological cholinergic synaptogenesis and remodeling, as well as pathological loss
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
I B Svendsen et al.
Carlsberg research communications, 54(6), 231-239 (1989-01-01)
A trypsin inhibitor with a Km of 5 x 10(-5) M has been isolated from kohlrabi (Brassica napus var. rapifera). Subtilisin DY is inhibited only weakly and chymotrypsin not at all. The inhibitor is closely related to napin as determined
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

Protocolos

Trypsin Inhibitors

Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

Trypsin Inhibitors

Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

Trypsin Inhibitors

Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

Trypsin Inhibitors

Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

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