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Proteinase K NGS grade was developed for highly demanding applications. Special purification technology achieves significantly increased solubility (2.5-fold over our standard proteinase K), increased specific activity and exceptional purity at a DNA content of ≤0.1pg/mg. Proteinase K NGS Grade is exonuclease free, endonucleases and ribonucleases.
Proteinase K from Tritirachium album belongs to the familiy of subtilisin-like serine proteases. It has an endo- and exoproteolytic activity. Activated by calcium (1 - 5mM), Proteinase K exhibits a broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents after hydrophobic amino acids. Proteins will be completely digested, if the incubation time is long and the protease concentration high enough.
Inhibition/Inhibitors of Proteinase K
As Calcium is not directly involved in the catalytic process, removal of the Calcium ions will almost not influence the enzymatic activity but the stability of the enzyme is reduced (about 80% residual activity). The pH-optimum is at 8, but the enzyme is active over a wide pH-range (pH5 - 12). An elevation of the reaction temperature from 37°C to 50 - 60°C may increase the activity several times, like the addition of 0.5 - 1% SDS. Temperatures above 65°C, trichloroacetic acid or the serine protease inhibitors AEBSF (M6360) >, PMSF (M3194) > or DFP inhibit the activity.
Proteinase K will not be inhibited by EDTA, urea (1-4 M), SDS, citrate, iodoacetic acid or, interestingly, by other serine protease inhibitors like TLCK (M3375) > and TPCK (M3374) >. In case that proteinase K has to be inactivated, make sure, that the temperature is not below 95°C and the time not shorter than 10 minutes. A TCA-precipitation is well suited too.
Proteinase K is used for the digestion of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, since it very effectively inactivates DNases and RNases. The digest with Proteinase K for the purification of nucleic acids is performed in the presence of EDTA (inhibition of magnesium-dependent enzymes).
Appearance: white lyophilisate
Activity: > 45 U/mg Protein
DNA content: ≤0,1pg/mg Proteinase K NGS
DNAses and RNAses: not detectable
Solubility: easily soluble in water
application:Protein digest in DNA samples Isolation of genomic DNA from mouse tails Isolation of genomic DNA from cell cultures
Unit Definition:Activity: >45 U/mg protein. One unit of Proteinase K hydrolyzes urea-denaturated hemoglobin producing color equivalent of 1 μmol tyrosine per 1 min at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.
Sicherheits Hinweise / SafetyH-Sätze: H315, H319 ,H334, H335
GHS-Symbole: GHS07, GHS08
Klassifizierungen / ClassificationEC-Nr: 254-457-8
Dokumente - Protokolle - Downloads
Here you will find information and further literature on Proteinase K NGS grade - Powder. For further documents (certificates with additional lot numbers, safety data sheets in other languages, further product information) please contact Genaxxon biosience at: email@example.com or phone: +49 731 3608 123.
Hier finden Sie Artikel und Literaturzitate, in denen die Autoren auf die hohe Qualität dieses Genaxxonprodukts vertrauen.
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Alasdair W. Jubb, Shelagh Boyle, David A. Hume, Wendy A. Bickmore
Cell Rep. 2017 Dec 12; 21(11): 3022–3031. Published online 2017 Dec 12. doi: 10.1016/j.celrep.2017.11.053
Alasdair W Jubb, Robert S Young, David A Hume, Wendy A Bickmore
J Immunol. Author manuscript; available in PMC 2016 Jul 15.Published in final edited form as: J Immunol. 2016 Jan 15; 196(2): 813–822. Published online 2015 Dec 9. doi: 10.4049/jimmunol.1502009
Dhawal Jain, Sandro Baldi, Angelika Zabel, Tobias Straub, Peter B. Becker
Nucleic Acids Res. 2015 Aug 18; 43(14): 6959–6968. Published online 2015 Jun 27. doi: 10.1093/nar/gkv637
Henrike Klinker, Felix Mueller-Planitz, Renliang Yang, Ignasi Forné, Chuan-Fa Liu, Lars Nordenskiöld, Peter B. Becker
PLoS One. 2014; 9(2): e88411. Published online 2014 Feb 6. doi: 10.1371/journal.pone.0088411
Robert S. Illingworth, Catherine H. Botting, Graeme R. Grimes, Wendy A. Bickmore, Ragnhild Eskeland
PLoS One. 2012; 7(4): e34848. Published online 2012 Apr 9. doi: 10.1371/journal.pone.0034848
Ragnhild Eskeland, Anton Eberharter, Axel Imhof
Mol Cell Biol. 2007 Jan; 27(2): 453–465. Published online 2006 Nov 13. doi: 10.1128/MCB.01576-06