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Key Documents

T9767

Sigma-Aldrich

Trypsin inhibitor

powder, suitable for electrophoresis

Synonim(y):

SBTI

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About This Item

Numer CAS:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352200
NACRES:
NA.77

product name

Trypsin inhibitor from Glycine max (soybean), For use as a marker in SDS-PAGE, BioReagent

pochodzenie biologiczne

Glycine max (soybean)

Poziom jakości

linia produktu

BioReagent

Postać

powder

masa cząsteczkowa

20,000 Da

opakowanie

vial of 5 mg

metody

electrophoresis: suitable

rozpuszczalność

balanced salt solution: 1 mg/mL
concentrate: >10 mg/mL, hazy, amber-yellow
phosphate buffer: 10 mg/mL
water: 10 mg/mL
serum-free medium: soluble

Warunki transportu

ambient

temp. przechowywania

2-8°C

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Zastosowanie

Trypsin inhibitor from Glycine max (soybean) has been used as a standard molecular weight marker in electrophoresis.

Działania biochem./fizjol.

This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent.

Komponenty

The soybean trypsin inhibitor is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges.

Definicja jednostki

One trypsin unit = A253 of 0.001 per minute with N-alpha-benzoyl-L-arginine ethyl ester (BAEE) as substrate at pH 7.6 at 25 °C.
One trypsin unit = A253 of 0.001 per minute with N-alpha-benzoyl-L-arginine ethyl ester (BAEE) as substrate at pH 7.6 at 25 °C.

Uwaga dotycząca przygotowania

The trypsin inhibitor is soluble in water and phosphate buffers at 10 mg/mL. It is soluble in balanced salt solutions at 1 mg/mL and in serum-free media. Concentrated solutions greater than 10 mg/mL may be hazy and have a yellow to amber color. After trypsinizing cells, resuspend in 1 mL trypsin inhibitor solution at 1 mg/mL for every mL of trypsin solution used for dissociation. The cell suspension should then be centrifuged at 1000 rpm, forming a cell pellet.

Solutions can retain activity when stored short-term at 2-8° C. Solutions are stable in frozen aliquots at -20°C.
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produkt powiązany

Numer produktu
Opis
Cennik

Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1 - Skin Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
Godoy MS, et al.
Testing, 8(6), e66689-e66689 (2013)
Selective enrichment of albumin in biological samples by CE using segmental filling with sodium octyl sulfate in the background electrolyte
Lin Chin-Yu and Tseng Wei-Lung
Electrophoresis, 30(3), 532-539 (2009)
Quantification of tear proteins by SDS-PAGE with an internal standard protein: a new method with special reference to small volume tears
Li K, et al.
Graefe'S Archive For Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Fur Klinische Und Experimentelle Ophthalmologie, 248(6), 853-862 (2010)
Isabelle Le Potier et al.
Methods in molecular biology (Clifton, N.J.), 1466, 1-10 (2016-07-31)
Capillary electrophoresis (CE) coupled to fluorescence detection is an invaluable technique for the quantitative analysis of proteins of interest in the field of clinical diagnosis and quality control of novel biotechnology products. The various chemical and instrumental approaches that have
Martín S Godoy et al.
PloS one, 8(6), e66689-e66689 (2013-07-03)
Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands

Produkty

For use as a marker in SDS-PAGE; Albumin from chicken egg white, For use as a marker in SDS-PAGE; L-Lactic Dehydrogenase from rabbit muscle, Type XI, lyophilized powder, 600-1,200 units/mg protein

Protokoły

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.

Naturalne inhibitory trypsyny (serpiny) regulują aktywację i katabolizm białek poprzez hamowanie proteaz serynowych in vivo.

Chromatograms

application for HPLC

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