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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

CAS Number:
9035-81-8
MDL number:
MFCD00082102
UNSPSC Code:
12352204
NACRES:
NA.75

Quality Level

400

sterility

sterile-filtered

product line

BioReagent

form

solution

technique(s)

cell culture | mammalian: suitable

shipped in

dry ice

storage temp.

−20°C

Related Categories

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.

Physical form

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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pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Certificates of Analysis (COA)

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Jolanta Kamińska et al.
Advances in medical sciences, 64(2), 274-279 (2019-03-23)
In vitro expansion is an invaluable method to obtain keratinocytes in amounts necessary for effective transplantation therapies. In vitro cell culturing provokes questions concerning potential epigenetic alterations occurring in expanded cells in the context of usefulness for transplantation and safety.
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
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

Protocols

Trypsin Inhibitors

Natural trypsin Inhibitors also known as serine protease inhibitors (serpins) are the largest and most diverse family of protease inhibitors. Serpins control the activation and catabolism of proteins by the inhibition of serine proteases in vivo.

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