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Documentos Principais

T0699

Sigma-Aldrich

Trichloroacetic acid solution

6.1 N

Sinônimo(s):

TCA

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About This Item

Fórmula linear:
Cl3CCOOH
Número CAS:
Peso molecular:
163.39
Beilstein:
970119
Número MDL:
Código UNSPSC:
12352106
ID de substância PubChem:
NACRES:
NA.26

Formulário

liquid

Nível de qualidade

concentração

6.1 N
~100 % (w/v)

cadeia de caracteres SMILES

OC(=O)C(Cl)(Cl)Cl

InChI

1S/C2HCl3O2/c3-2(4,5)1(6)7/h(H,6,7)

chave InChI

YNJBWRMUSHSURL-UHFFFAOYSA-N

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Descrição geral

Trichloroacetic acid (TCA) is a strong acid. At the pH of drinking water, TCA exists almost in salt form.

Aplicação

Trichloroacetic acid solution has been used:
  • in indoleamine 2,3-dioxygenase (IDO) enzyme assay to hydrolyze N-formylkynurenine and produce kynurenine
  • in the proliferation of human pulmonary artery smooth muscle cells (HPASMCs)
  • to treat ground tissue and precipitate proteins during protein extraction and quantification

Ações bioquímicas/fisiológicas

Trichloroacetic acid solution is traditionally used to precipitate protein. It can be used to determine protein concentration by quantitative precipitation. Trichloroacetic acid can also be used as a decalcifier and fixative in microscopy.
Trichloroacetic acid (TCA) with no known systemic toxicity, is used as a time-honored agent for superficial peeling. It is a peroxisome proliferator.

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

Aquatic Acute 1 - Aquatic Chronic 1 - Eye Dam. 1 - Skin Corr. 1A - STOT SE 3

Órgãos-alvo

Respiratory system

Código de classe de armazenamento

8A - Combustible corrosive hazardous materials

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Guillaume Laflamme et al.
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The segregation of chromosomes is a critical step during cell division. This process is driven by the elongation of spindle microtubules and is tightly regulated by checkpoint mechanisms. It is unknown whether microtubules affect checkpoint responses as passive contributors or
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Diabetes, 63(8), 2643-2655 (2014-03-13)
After diabetes, the heart has a singular reliance on fatty acid (FA) for energy production, which is achieved by increased coronary lipoprotein lipase (LPL) that breaks down circulating triglycerides. Coronary LPL originates from cardiomyocytes, and to translocate to the vascular
Verena Pfahler et al.
The New phytologist, 197(1), 186-193 (2012-10-31)
The objective of this study was to investigate the isotopic composition of oxygen bound to phosphate (δ(18)O-PO(4)) in different phosphorus (P) pools in plant leaves. As a model plant we used soybean (Glycine max cv Toliman) grown in the presence
Inga Müller et al.
PloS one, 9(5), e97285-e97285 (2014-05-27)
Members of the MYC family are the most frequently deregulated oncogenes in human cancer and are often correlated with aggressive disease and/or poorly differentiated tumors. Since patients with MYCN-amplified neuroblastoma have a poor prognosis, targeting MYCN using small molecule inhibitors

Artigos

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).

Protocolos

This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.

To standardize a procedure for the determination of the enzymatic assay of choloylglycine hydrolase.

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).

To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate at Sigma-Aldrich St. Louis.

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