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Merck
CN

T7659

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
UNSPSC Code:
12352204
NACRES:
NA.75
MDL number:
MFCD00082102

Key Documents

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Product Name

Trypsin Inhibitor, Defined (1X) Solution, Animal component free, BioReagent, suitable for cell culture

sterility

sterile-filtered

product line

BioReagent

form

solution

technique(s)

cell culture | mammalian: suitable

shipped in

dry ice

storage temp.

−20°C

Quality Level

400

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.

Preparation Note

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Regulatory Information

动植物源性产品
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Certificates of Analysis (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
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 (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

胰蛋白酶抑制剂

天然胰蛋白酶抑制剂也称为丝氨酸蛋白酶抑制剂（serpins），是最大和最多样化的蛋白酶抑制剂家族。Serpins通过抑制体内丝氨酸蛋白酶来控制蛋白质的活化和分解代谢。

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