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P5568

Sigma-Aldrich

Proteinase K from Tritirachium album

≥500 units/mL, buffered aqueous glycerol solution

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Synonym(s):
Endopeptidase K
CAS Number:
Enzyme Commission number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

biological source

microbial (T.album
T. ALBUM)

Quality Level

form

buffered aqueous glycerol solution

mol wt

28.93 kDa

concentration

≥10 mg/mL
≥500 units/mL

technique(s)

DNA extraction: suitable

storage temp.

2-8°C

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This Item
SRE0047SAE0009P8044
technique(s)

DNA extraction: suitable

technique(s)

-

technique(s)

DNA extraction: suitable

technique(s)

DNA extraction: suitable

concentration

≥10 mg/mL, ≥500 units/mL

concentration

-

concentration

-

concentration

-

form

buffered aqueous glycerol solution

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

mol wt

28.93 kDa

General description

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.

Application

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.

Biochem/physiol Actions

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.

Unit Definition

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).

Physical form

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

Preparation Note

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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
Role of apoptosis in erosive and reticular oral lichen planus exhibiting variable epithelial thickness
Brant JMC, et al.
Brazilian Dental Journal, 19(3) (2008)
Young S Oh et al.
American journal of physiology. Cell physiology, 289(3), C576-C581 (2005-04-22)
The polytopic membrane protein presenilin 1 (PS1) is a component of the gamma-secretase complex that is responsible for the intramembranous cleavage of several type I transmembrane proteins, including the beta-amyloid precursor protein (APP). Mutations of PS1, apparently leading to aberrant
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)

Protocols

Proteinase K activity measured via spectrophotometry using hemoglobin substrate, crucial for enzyme characterization.

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