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P5568

Sigma-Aldrich

Proteinasa K from Tritirachium album

≥500 units/mL, buffered aqueous glycerol solution

Sinónimos:

Endopeptidasa K

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About This Item

Número de CAS:
39450-01-6
Comisión internacional de enzimas:
3.4.21.64 (BRENDA, IUBMB)
Número MDL:
MFCD00132129
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

origen biológico

microbial (T.album
T. ALBUM)

Nivel de calidad

200

formulario

buffered aqueous glycerol solution

mol peso

28.93 kDa

concentración

≥10 mg/mL
≥500 units/mL

técnicas

DNA extraction: suitable

temp. de almacenamiento

2-8°C

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Descripción general

Proteinase K, an extracellular endopeptidase is synthesized by the mold, Tritirachium album Limber. Proteinase K belongs to a new subfamily of the subtilisins. It is a 277 amino acid protein and is characterized with an unhydrolyzed protein chain and autolyzed polypeptide chains.

Aplicación

Útil para la inactivación proteolítica de nucleasas durante el aislamiento de ADN y ARN.
Elimina las endotoxinas que se unen a las proteínas catiónicas como la lisozima y la ribonucleasa A.
Se ha comunicado que es útil para el aislamiento de mitocondrias hepáticas, de levadura y de frijol mung
Determinación de la localización de las enzimas en las membranas
Tratamiento de cortes de tejido incluidos en parafina para exponer los sitios de unión de antígenos para el marcado con anticuerpos.
Digestión de proteínas de muestras de tejido cerebral para investigación de los priones en las encefalopatías espongiformes transmisibles (EET).
Proteinase K from Tritirachium album has been used:
  • to break down cardiac muscle during histopathology studies
  • during the digestion of HEK-293 cells
Proteinase K from Tritirachium album has been used in in situ detection of DNA fragmentation and in proteolysis experiments to measure the structural flexibility of interleukin 1ra (IL-1ra).
The enzyme from Sigma has been used in the digestion of sealed cytosolic side out ER vesicles. It has been used to deproteinize dissected brain and/or whole pupae sections of honey bee prior to in situ hybridisation. This was done during the study of neuropeptide Y-like signaling, and nutritionally-mediated gene expression and behaviour in the honey bee.

Acciones bioquímicas o fisiológicas

Proteinase K has a broad specificity and degrades many proteins even in the native state. It mainly cleaves the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha-amino groups. The optimum pH is between 7.5-9.0 and the isoelectric point is 8.9. Ca2+ (1-5 mM) is required for activation. Proteinase K is inhibited by DIFP or PMSF.
La proteinasa K es una serín proteasa estable y muy reactiva. La evidencia procedente de estudios de la estructura cristalina y molecular indica que la enzima pertenece a la familia subtilisina con una tríada catalítica en el sitio activo (ASP39-HIS69-ser224). Es estable en una amplia variedad de entornos: pH, sales amortiguadoras, detergentes (SDS) y temperatura. En presencia de SDS al 0,1 - 0,5 %, la proteinasa K conserva su actividad y digerirá una variedad de proteínas y nucleasas en preparaciones de ADN sin comprometer la integridad del ADN aislado.

Definición de unidad

One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

Forma física

Solution in 40% (v/v) glycerol containing 10 mM Tris-HCl, pH 7.5, with 1 mM calcium acetate.

Nota de preparación

Proteinase K in solution is stable over a pH range of 4.0-12.5 (optimum pH 8.0), and is also stable over the temperature range of 25°C to 65°C during use. At pH 8.0, solutions will be stable for at least 12 months at 4°C. At pH 4-11.5, solutions containing Ca2+ (1-6 mM) are expected to be stable for several weeks. An 80% ammonium sulfate suspension stored at 4°C is stable for at least 12 months.

Pictogramas

Health hazard
GHS08

Palabra de señalización

Danger

Frases de peligro

H334

Consejos de prudencia

P261 - P284 - P501

Clasificaciones de peligro

Resp. Sens. 1

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Denaturant-Dependent Conformational Changes in a beta-Trefoil Protein: Global and Residue-Specific Aspects of an Equilibrium Denaturation Process
Latypov RF, et al.
Biochemistry, 48(46), 10934-10947 (2009)
Amino acid sequence of proteinase K from the mold Tritirachium album Limber
Jany KD, et al.
Febs Letters, 199(2), 139-144 (2001)
Carolina Rosa Gioda et al.
American journal of physiology. Heart and circulatory physiology, 298(6), H2039-H2045 (2010-03-23)
Thiamine is an important cofactor of metabolic enzymes, and its deficiency leads to cardiovascular dysfunction. First, we characterized the metabolic status measuring resting oxygen consumption rate and lactate blood concentration after 35 days of thiamine deficiency (TD). The results pointed
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Previous research has led to the idea that derived traits can arise through the evolution of novel roles for conserved genes. We explored whether neuropeptide Y (NPY)-like signalling, a conserved pathway that regulates food-related behaviour, is involved in a derived
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Artículos

Enzymatic Assay of Proteinase K with Hemoglobin Substrate

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).

Enzymatic Assay of Proteinase K with Hemoglobin Substrate

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

Enzymatic Assay of Proteinase K (EC 3.4.21.64)

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).

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