T7659
Trypsin Inhibitor, Defined (1X) Solution
Animal component free, BioReagent, suitable for cell culture
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Doporučené produkty
Quality Level
sterility
sterile-filtered
product line
BioReagent
form
solution
technique(s)
cell culture | mammalian: suitable
shipped in
dry ice
storage temp.
−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.
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.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
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
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
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
Protokoly
Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.
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