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P5568

Sigma-Aldrich

Proteinase K from Tritirachium album

≥500 units/mL, buffered aqueous glycerol solution

Synonim(y):

Endopeptidase K

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About This Item

Numer CAS:
39450-01-6
Numer EC enzymu:
3.4.21.64 (BRENDA, IUBMB)
Numer MDL:
MFCD00132129
Kod UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

pochodzenie biologiczne

microbial (T.album
T. ALBUM)

Poziom jakości

200

Postać

buffered aqueous glycerol solution

masa cząsteczkowa

28.93 kDa

stężenie

≥10 mg/mL
≥500 units/mL

metody

DNA extraction: suitable

temp. przechowywania

2-8°C

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Opis ogólny

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.

Zastosowanie

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.
Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.
Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria
Determination of enzyme localization on membranes
Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.
Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

Działania biochem./fizjol.

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.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

Definicja jednostki

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).

Postać fizyczna

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

Uwaga dotycząca przygotowania

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.
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Piktogramy

Health hazard
GHS08

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

H334

Zwroty wskazujące środki ostrożności

P261 - P284 - P501

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

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

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
Role of apoptosis in erosive and reticular oral lichen planus exhibiting variable epithelial thickness
Brant JMC, et al.
Brazilian Dental Journal, 19(3) (2008)
S A Ament et al.
Insect molecular biology, 20(3), 335-345 (2011-02-26)
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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Produkty

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).

Protokoły

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).

Test enzymatyczny proteinazy K

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

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