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Merck
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Key Documents

T7659

Sigma-Aldrich

Trypsin Inhibitor, Defined (1X) Solution

Animal component free, BioReagent, suitable for cell culture

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About This Item

Numéro CAS:
9035-81-8
Numéro MDL:
MFCD00082102
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.75

Niveau de qualité

400

Stérilité

sterile-filtered

Gamme de produits

BioReagent

Forme

solution

Technique(s)

cell culture | mammalian: suitable

Conditions d'expédition

dry ice

Température de stockage

−20°C

Application

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.

Forme physique

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

Reconstitution

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

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Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H317,H334

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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

Protocoles

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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