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Sigma-Aldrich

Trypsin inhibitor

powder, suitable for isoelectric focusing (IEF)

Sinônimo(s):

SBTI

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About This Item

Número CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352200
NACRES:
NA.77

R$ 409,00


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Nome do produto

Trypsin inhibitor from Glycine max (soybean), Isoelectric focusing marker, pI 4.6

fonte biológica

Glycine max (soybean)

Nível de qualidade

Formulário

powder

peso molecular

20,100 Da

técnica(s)

isoelectric focusing (IEF): suitable

pI 

4.6

solubilidade

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

Condições de expedição

ambient

temperatura de armazenamento

−20°C

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Ações bioquímicas/fisiológicas

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.

Componentes

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

Definição da unidade

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.

Nota de preparo

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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Amaury Pereira-Acácio et al.
PloS one, 17(8), e0273385-e0273385 (2022-08-20)
We investigated the mechanisms by which chronic administration of a multideficient diet after weaning alters bodily Na+ handling, and culminates in high systolic blood pressure (SBP) at a juvenile age. From 28 to 92 days of age, weaned male Wistar
Kine Gregersen et al.
International journal of general medicine, 4, 555-560 (2011-09-03)
Food hypersensitivity is commonly suspected, but seldom verified. Patients with subjective food hypersensitivity suffer from both intestinal and extraintestinal health complaints. Abnormalities of the enterochromaffin cells may play a role in the pathogenesis. The aim of this study was to
Astrid F Nottebaum et al.
The Journal of experimental medicine, 205(12), 2929-2945 (2008-11-19)
We have shown recently that vascular endothelial protein tyrosine phosphatase (VE-PTP), an endothelial-specific membrane protein, associates with vascular endothelial (VE)-cadherin and enhances VE-cadherin function in transfected cells (Nawroth, R., G. Poell, A. Ranft, U. Samulowitz, G. Fachinger, M. Golding, D.T.
Humberto Muzi-Filho et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 54(6), 1143-1162 (2020-11-18)
Chronic malnutrition (M) affects >1 billion people worldwide. Epidemiological data point to long-term renal and cardiovascular outcomes (e.g. arterial hypertension, cardiorenal syndromes). The renin-angiotensin-aldosterone system (RAAS) has been implicated in the physiopathology of these disturbances, but M-induced alterations in RAAS-modulated
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

Protocolos

Natural trypsin inhibitors (serpins) regulate protein activation and catabolism by inhibiting serine proteases in vivo.

Chromatograms

application for HPLC

Questions

1–2 of 2 Questions  
  1. What is the Department of Transportation shipping information for this product?

    1 answer
    1. Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.

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  2. What is the molecular weight and amino acid sequence of trypsin inhibitor from Glycine max (soybean)?

    1 answer
    1. Soybean trypsin inhibitor is a mixture of the three types. We have not characterized our trypsin inhibitor products in terms of how much of each of the three types may be present. All three have a molecular weight of between 20,000 and 20,200 daltons, so one might use 20,100 daltons as an average.The three types vary in the amino acids at a few positions. The detailed summary of the three types (or variants) was published in the following linked reference:     J. Biochem. (Japan), 98, 435-448 (1985).Note that the authors use Tia, Tib and Tic to indicate the three variants.

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