Összes fotó(1)
Fontos dokumentumok
E0885
Enterokinase from porcine intestine
lyophilized powder, ≥100 units/mg protein
Szinonimák:
Enteropeptidase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
![4-(N-[2,4-Diamino-6-pteridinylmethyl]amino)benzoic acid sodium salt ≥95% (TLC)](/deepweb/assets/sigmaaldrich/product/structures/855/619/06a9574b-3e45-48aa-85c1-2f25917fa5a7/640/06a9574b-3e45-48aa-85c1-2f25917fa5a7.png)
form
lyophilized powder
Minőségi szint
specifikus aktivitás
≥100 units/mg protein
molekulatömeg
150 kDa
tisztítva
chromatography
összetétel
Protein, ≥20% Lowry
idegen aktivitás
aminopeptidase ≤1.5%
trypsin ≤1%, free
tárolási hőmérséklet
−20°C
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Alkalmazás
Enterokinase from porcine intestine has been used in a study to investigate complementary DNA cloning and sequencing of rat enteropeptidase. Enterokinase from porcine intestine has also been used to learn more about the insulinotropic region of the gastric inhibitory polypeptide.
The enzyme from Sigma has been used to activate zymogens in order to detect trypsin activity. The study to investigated the structural and evolutionary consequences of unpaired cysteines in trypsinogen. The product has been used to measure trypsin while studying the effect of pesticide induced alterations in gene expression in the lobster, Homarus americanus The enzyme from Sigma has been used to develop a novel assay for measuring levels of lipid-free apoA-I in the presence of lipid-bound apoA-I. Enteropeptidase can specifically cleave human lipid-free apoA-I but not its lipid-bound form resulting in an N-terminal fragment of 22 kDa. It has also been used in a study to examine the effect of calcium and phytic acid on the activation of trypsinogen and the stability of trypsin.
Biokémiai/fiziológiai hatások
Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer consisting of 35-47 kDa subunits. The light and the heavy chains are linked by two disulfide bridges. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)4-Lys- sequence. The enzyme is inhibited by soybean trypsin inhibitor. Enterokinase is typically used in protein modification and amino acid sequence determination.
Egység definíció
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.
Fizikai forma
Lyophilized powder containing sodium phosphate buffer salts
szubsztrát
Product No.
Leírás
Árazás
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 3
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
Eyeshields, Gloves, type N95 (US)
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Effect of calcium and phytic acid on the activation of trypsinogen and the stability of trypsin.
Caldwell RA
Journal of Agricultural and Food Chemistry, 40 (1), 43-46 (1992)
Michael N Horst et al.
Comparative biochemistry and physiology. Part D, Genomics & proteomics, 2(1), 44-52 (2007-03-01)
Using subtractive hybridization, we have identified 17 genes that are either up- or down-regulated in the hepatopancreas (Hp) of the lobster, Homarus americanus, by acute exposure to the juvenile hormone analog methoprene. The expression of some of the genes obtained
W Safi et al.
Journal of lipid research, 42(5), 864-872 (2001-05-16)
Recent studies indicate that certain lipid-poor forms of apolipoprotein (apo)A-I may be particularly important in promoting cholesterol release from overburdened cells in the periphery. However, a detailed understanding of the physiological relevance of these species has been hampered by the
G W Morrow et al.
Canadian journal of physiology and pharmacology, 74(1), 65-72 (1996-01-01)
Glucose-dependent insulinotropic polypeptide or gastric inhibitory polypeptide (GIP) is a 42 amino acid intestinal hormone, which exhibits several direct and indirect effects on fat and glucose metabolism. To determine the bioactive region(s) of the molecule, synthetic and proteolytic fragments of
Complementary DNA cloning and sequencing of rat enteropeptidase and tissue distribution of its mRNA.
N Yahagi et al.
Biochemical and biophysical research communications, 219(3), 806-812 (1996-02-27)
A cDNA clone encoding enteropeptidase (EC 3.4.21.9), a key enzyme for the conversion of trypsinogen to trypsin, was isolated from a rat duodenal mucosa cDNA library. Sequences of the 3585 base pair clone predicted that enteropeptidase is synthesized as a
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