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T0581

Sigma-Aldrich

Transglutaminase from guinea pig liver

≥1.5 units/mg protein, recombinant, expressed in E. coli

Sinônimo(s):

TGase

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About This Item

Número da licença da enzima:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in E. coli

Nível de qualidade

atividade específica

≥1.5 units/mg protein

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

Aplicação

10 mM calcium chloride is used for activation of the enzyme.
Transglutaminase has been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.Transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity.

Definição da unidade

One unit will catalyze the formation of 1.0 μmole of hydroxamate per minute from Nα-Z-Gln-Gly and hydroxylamine at pH 6.0 at 37 °C. (L-Glutamic acid γ-monohydroxamate is the standard.)

forma física

Lyophilized from 10 mM NaH2PO4, 150 mM NaCl, pH 8. Contains maltodextrin.

Pictogramas

Exclamation mark

Palavra indicadora

Warning

Frases de perigo

Classificações de perigo

Eye Irrit. 2

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Sigma-Aldrich

T3824

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Acyl-CoA esters of xenobiotic carboxylic acids as biochemically active intermediates.
H S Sherratt
Biochemical Society transactions, 13(5), 856-858 (1985-10-01)
S Kølvraa et al.
Biochemical medicine and metabolic biology, 36(1), 98-105 (1986-08-01)
Prompted by the fact that the urinary excretion of organic acids in the riboflavin-deficient rat closely mimics that found in patients with inborn errors in the acyl-CoA dehydrogenation systems, the organelle localization and the apparent kinetic constants (Km and Vmax
K D MacDermot et al.
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We report investigations of benzoate and glycine metabolism and glycine acyltransferase activity in rats. These studies provide insights related to the therapy and pathophysiology of human nonketotic hyperglycinemia. Liver acyltransferase activity increased sharply postnatally from low levels at birth, but
M Kelley et al.
Journal of biochemical toxicology, 5(2), 125-135 (1990-01-01)
The aralkyl-CoA:glycine N-acyltransferase and the arylacetyl-CoA:amino acid of N-acyltransferase were purified from bovine liver mitochondria and their response to a variety of ions investigated. The activity of the aralkyl transferase was inhibited by divalent cations with all substrates investigated. For
C M Becker et al.
Archives of biochemistry and biophysics, 223(2), 381-392 (1983-06-01)
Valproic acid (dipropylacetic acid), an antiepileptic agent known to be hepatotoxic in some patients, caused inhibition of lactate gluconeogenesis, fatty acid oxidation, and fatty acid synthesis by isolated hepatocytes. The latter process was the most sensitive to valproic acid, 50%

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