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Merck

U1250

Sigma-Aldrich

Urea

ReagentPlus®, ≥99.5%, pellets

Synonim(y):

Carbamide, Carbonyldiamide

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About This Item

Wzór liniowy:
NH2CONH2
Numer CAS:
Masa cząsteczkowa:
60.06
Beilstein:
635724
Numer WE:
Numer MDL:
Kod UNSPSC:
12352100
Identyfikator substancji w PubChem:
NACRES:
NA.21

Poziom jakości

linia produktu

ReagentPlus®

Próba

≥99.5%

Postać

pellets

mp

132-135 °C (lit.)

rozpuszczalność

H2O: 8 M

gęstość

1.335 g/mL at 25 °C (lit.)

ciąg SMILES

NC(N)=O

InChI

1S/CH4N2O/c2-1(3)4/h(H4,2,3,4)

Klucz InChI

XSQUKJJJFZCRTK-UHFFFAOYSA-N

informacje o genach

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Opis ogólny

Urea is a chaotropic agent and is used for protein denaturation. It disturbs the hydrogen bonds in the secondary, tertiary and quaternary structure of proteins. Urea can also disturb hydrogen bonds present in DNA secondary structure.

Zastosowanie

Urea has been used as a protein denaturing agent.
Used for the denaturation of proteins and as a mild solubilization agent for insoluble or denatured proteins. Useful for renaturing proteins from samples already denatured with 6 M guanidine chloride such as inclusion bodies. May be used with guanidine hydrochloride and dithiothreitrol (DTT) in the refolding of denatured proteins into their native or active form.

Informacje prawne

ReagentPlus is a registered trademark of Merck KGaA, Darmstadt, Germany
This page may contain text that has been machine translated.

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


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SAFC

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Sheehan D.
Physical Biochemistry: Principles and Applications (2013)
Protein carbonyl determination by a rhodamine B hydrazide-based fluorometric assay.
Georgiou C D, et al.
Redox Biology, 17, 236-245 (2018)
Protein and cell wall polysaccharide carbonyl determination by a neutral pH 2, 4-dinitrophenylhydrazine-based photometric assay.
Georgiou C D, et al.
Redox Biology, 17, 128-142 (2018)
Christos D Georgiou et al.
Redox biology, 17, 128-142 (2018-04-24)
A new 2,4-dinitrophenylhydrazine (DNPH)-based photometric assay is developed for the quantification of carbonyls in protein samples from any biological source by protein carbonyl-DNPH hydrazone formation at acidic pH in the presence of denaturing urea, and subsequent hydrazone solubilization in the
Gurudayal et al.
Nano letters, 15(6), 3833-3839 (2015-05-06)
Photoelectrochemical water splitting half reactions on semiconducting photoelectrodes have received much attention but efficient overall water splitting driven by a single photoelectrode has remained elusive due to stringent electronic and thermodynamic property requirements. Utilizing a tandem configuration wherein the total

Produkty

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Protokoły

Enzymatic Assay of Urease from Jack Beans

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Aktywność proteinazy K mierzona za pomocą spektrofotometrii przy użyciu substratu hemoglobiny, kluczowa dla charakterystyki enzymu.

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