Merck
CN
All Photos(3)

Documents

Safety Information

P8044

Sigma-Aldrich

Proteinase K from Tritirachium album

≥3.0 unit/mg solid, lyophilized powder

Sign Into View Organizational & Contract Pricing
All Photos(3)
Synonym(s):
Endopeptidase K
CAS Number:
39450-01-6
Enzyme Commission number:
3.4.21.64 (BRENDA, IUBMB)
EC Number:
254-457-8
MDL number:
MFCD00132129
eCl@ss:
32160410
NACRES:
NA.54

biological source

maize
microbial (T.album
T. ALBUM)
plant seeds (barley)
soybean
yeast

Quality Level

200

form

lyophilized powder

specific activity

≥3.0 unit/mg solid

mol wt

28.93 kDa

composition

Protein, ≥15% biuret

technique(s)

DNA extraction: suitable

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

Application

Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. It is used for the removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A. It is also useful for the isolation of hepatic, yeast, and mung bean mitochondria and is used to determine enzyme localization on membranes. Furthermore, it is used for the treatment of paraffin embedded tissue sections to expose antigen binding sites and for digestion of proteins from brain tissue samples. Product P8044 is provided as a lyophilized powder.
The enzyme from Sigma has been used to degrade complex I (NADH:ubiquinone oxidoreductase) prior to extraction of ubiquinone from Yarrowia lipolytica. It has been used to examine the effect of Proteinase k on Pythium ultimum. It has also been used to maximize the variety of peptide bonds hydrolyzed in the sediment slurry without autolytic production of amino acids from the enzyme itself.
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 is highly active towards native proteins. It 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 α-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 diisopropyl fluorophosphate (DFIP), and phenylmethanesulfonyl fluoride (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).

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Documents related to the products that you have purchased in the past have been gathered in the Document Library for your convenience.

Visit the Document Library

Difficulty Finding Your Product Or Lot/Batch Number?

Product numbers are combined with Pack Sizes/Quantity when displayed on the website (example: T1503-25G). Please make sure you enter ONLY the product number in the Product Number field (example: T1503).

Example:

T1503
Product Number
-
25G
Pack Size/Quantity

Additional examples:

705578-5MG-PW

PL860-CGA/SHF-1EA

MMYOMAG-74K-13

1000309185

enter as 1.000309185)

Having trouble? Feel free to contact Technical Service for assistance.

Lot and Batch Numbers can be found on a product's label following the words 'Lot' or 'Batch'.

Aldrich Products

  • For a lot number such as TO09019TO, enter it as 09019TO (without the first two letters 'TO').

  • For a lot number with a filling-code such as 05427ES-021, enter it as 05427ES (without the filling-code '-021').

  • For a lot number with a filling-code such as STBB0728K9, enter it as STBB0728 without the filling-code 'K9'.

Not Finding What You Are Looking For?

In some cases, a COA may not be available online. If your search was unable to find the COA you can request one.

Request COA

Yuanjun Lu et al.
Journal of experimental & clinical cancer research : CR, 41(1), 3-3 (2022-01-05)
Drug resistance to sorafenib greatly limited the benefits of treatment in patients with hepatocellular carcinoma (HCC). MicroRNAs (miRNAs) participate in the development of drug resistance. The key miRNA regulators related to the clinical outcome of sorafenib treatment and their molecular
C Dunne et al.
Microbiology (Reading, England), 146 ( Pt 8), 2069-2078 (2000-08-10)
Stenotrophomonas maltophilia W81 can protect sugar beet against PYTHIUM:-mediated damping-off disease through the production of an extracellular protease. Here, the proteolytic enzyme of W81 was purified by anion-exchange chromatography and characterized as a serine protease. The purified enzyme was fungicidal
P Bermejo-Alvarez et al.
Biology of reproduction, 79(4), 594-597 (2008-06-27)
It has been reported that the mammalian female could have a preconceptual influence on the sex of her offspring, and it has been hypothesized that this influence could go some way toward accounting for the reported lower fertility following insemination
Bioavailable amino acids in sediments: A biomimetic, kinetics-based approach
Mayer LM, et al.
Limnology and Oceanography, 40(3), 511-520 (1995)
Ivonne Gamper et al.
Scientific reports, 7(1), 9932-9932 (2017-09-01)
While genetically engineered mice have made an enormous contribution towards the elucidation of human disease, it has hitherto not been possible to tune up or down the level of expression of any endogenous gene. Here we describe compound genetically modified
View All Related Papers

Articles

Proteinase K: Introduction & Applications

Proteinase K aids in molecular biology applications by digesting structural proteins, removing nucleases, and isolating intact genomic DNA.

How Proteinase K Can Be Used in Tissue Samples

The use of Pro K in combination with other reagents, such as detergents and chaotropic agents, can help to disrupt the cell membranes and release DNA from tissue. This is particularly important for downstream applications such as PCR, sequencing, and other molecular biology techniques that require pure and intact DNA.

How Proteinase K Can Be Used in Blood DNA Extraction Applications

In blood DNA extraction, Proteinase K, an enzyme commonly used to degrade proteins, can help break down the cellular and nuclear membranes, releasing DNA from the cells that protect it from degradation and increase purity/yield making it more suitable for various molecular biology techniques.

How to Determine the Best Product & Supplier for Proteinase K

The cost of proteinase K can vary depending on the source, purity, manufacturing process and vendor’s quality management system. It is important to balance the cost with the desired quality, performance, documentation and technical/quality support to select the optimal Proteinase K for the intended application

See All

Protocols

Proteinase K Enzymatic Assay

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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service