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Proteinase K
[P1265]
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Alternative Product ID: Proteinase K, Tritirachium album, PK
Description: Porteinase K (also known as endopeptidase K) is an extracellular endopeptidase isolated from a culture filtrate of the fungus Tritirachium album limber. This fungus is able to grow on Keratin as the sole source of carbon and nitrogen and therefore given the K designation 1. Proteinase K is a member of the class of serine proteases 2. Since the sequence of the polypeptide chain of 279 amino acids in length 3 and the three dimensional structure 4 has a high degree of homology to bacterial subtilisins, Proteinase K is classified as a member of the subtilisin family. Proteinase K has a specific activity of more than 30 U/mg and is thus one of the most active of the known endopeptidases 5 and unspecifically hydrolyses native and denatured proteins.
DNAse/RNAse Activity: DNAse ACTIVITY: No detectable nicking activity with pBR322 after incubation for 6 hour at 37°C. RNAse ACTIVITY: No detectable ribonuclease activity after incubation for 16 hour at 25°C.
Molecular Weight: 28,500
E.C. NUMBER:: 3.4.21.14
CAS Number: CAS [39450-01-6]
Active Product: Yes
Appearance: Lyophilized powder
Activity: >30 units/mg solid. One unit is defined as the amount of enzyme that will liberate 1.0 mmol of tyrosine per minute at 37°C, pH 7.5. Proteinase K is active with or without the presence of SDS, EDTA and Urea. Proteinase K is inactivated by PMSF, AEBSF, or DFP
Handling: Store in a tightly sealed vial. Wear gloves and mask when handling this product. Avoid all modes of contact.
Storage: +4°C.
Shipping: Express Courier
Bulk Quantity: Readily Available
Applications:
• Purification of nucleic acids by degradation of contaminating proteins in yeast (Holm, C., et al. (1986) Gene. 42, 169-173), bacteria (Hansen, J., et al. (1974) Prep. Biochem. 4, 473-488), mammalian cell lysates (Kasche, V., et al. (1981) Prep. Biochem. 11, 233-250) and plant tissue lysates (Guidet, et al. (1994) Nucleic Acids. Res. 21, 4153-4154).
• Rapidly inactivates nucleases such as DNase and RNase when isolating RNA and high molecular weight DNA from tissues and cell lines (Weigers, U., et al. (1972) FEBS Lett. 23, 77).
• Removes nucleases in the preparation of tissue sections for in situ hybridization (Angerer, L. M., et al. (1987) Methods. Enzymol. 152, 649).
• Improves cloning efficiency of PCR products (Crowe, J. S., et al. (1991) Nucleic Acids Res. 19, 184).
• Preparing chromosomal DNA for pulsed field gel electrophoresis (Schwartz, D., et al. (1984) Cell. 37, 67).
• Preparing chromosomal DNA for protein finger printing (Cleveland, D. W., et al. (1977) J. Biol. Chem. 252, 1102-6).
• Specifically modifies cell surface proteins and glycoproteins for analysis of membrane structures for protein localization (Brdiczka, D., et al. (1973) Biochem. Biophys. Acta. 297, 203-212).
• Produces characteristic protein fragments used in enzyme/protein structure and function studies (Williamson, J., et al. (1977) Biochem. J. 167, 731-737).
• Inactivation of enzyme cocktails in ribonuclease protection assays (Bordonaro, M., et al. (1994) Biotechniques. 16, 428-430).
• Recently Proteinase K has been used for the detection of BSE proteins which are uniquely resistant to proteolytic degradation (Grassi, J., et al. (2000) Arch. Virol. Suppl. 16, 197-205).
• Proteinase K tissue digestion was used as an alternative sample preparation approach for quantitative analysis using liquid chromatography-tandem mass spectrometry (Yu, C., et al. (2004) Anal. Chem. 76, 1761-1767).
• Proteinase K added to the extraction procedure markedly increased RNA yields from primary breast tumors for use in microarray studies (Egyhazi, S., et al. (2004) Clin. Chem. 50, 975-976).
• DNA isolation and sample preparation for quantification of adduct levels by accelerator mass spectrometry (Dingley, K. H., et al. (2005) Methods. Mol. Biol. 291, 21-27).
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Note: All products sold by A.G. Scientific are for Laboratory or Manufacturing purposes only. They are not intended for Human Drug, Food Additive, Clinical or Household use.
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