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Proteinase K, recombinant
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Invitrogen™

Proteinase K, recombinant

Proteinase K from the fungus Engyodontium album is a nonspecific serine protease that is useful for general digestion of proteins.ProteinaseRead more
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Catalog NumberQuantity
255300311 g
25530015100 mg
Catalog number 25530031
Price (EUR)
1.864,65
Online Exclusive
1.984,00
Save 119,35 (6%)
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1 g
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Price (EUR)
1.864,65
Online Exclusive
1.984,00
Save 119,35 (6%)
Each
Add to cart
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Proteinase K from the fungus Engyodontium album is a nonspecific serine protease that is useful for general digestion of proteins.

Proteinase K remains active:
• Over a wide pH range–optimal activity between 6.5 and 9.5
• Under denaturing conditions–e.g., in the presence of SDS or urea
• In the presence of metal chelating agents—e.g., EDTA
• At comparatively high temperatures–optimum digestion temperature is 65°C

Applications
Removal of endogenous nucleases during the preparation of DNA and RNA; preparation of tissue sections for in situ hybridization.

Performance and quality testing
Endodeoxyribonuclease and exodeoxyribonuclease assays; liquid form tested for absence of RNase activity.

Unit definition
One mAnson unit is described as that amount of enzyme that liberates 1 μmol of Folin-positive amino acid within 1 min at 37°C using hemoglobin as a substrate.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Product TypeProteinase K
Quantity1 g
Shipping ConditionApproved for shipment at Room Temperature or on Wet Ice
Concentration>40 U/mg
FormPowder
Unit SizeEach
Contents & Storage
One tube Proteinase K
Store in refrigerator (2–8°C).
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Certificates

Lot #Certificate TypeDateCatalog Number(s)
47890424Certificate of AnalysisFeb 03, 202525530015
47891024Certificate of AnalysisJan 06, 202525530031
50320724Certificate of AnalysisAug 09, 202425530015
24001023Certificate of AnalysisApr 24, 202425530031
34410723Certificate of AnalysisMar 25, 202425530015
5 results displayed, search above for a specific certificate

Safety Data Sheets

Frequently asked questions (FAQs)

We recommend storing it at 4°C.

Scrape a single colony from the surface of an agar plate and transfer to 12 µL of SCL solution [10 mM Tris-HCl (pH 7.5), 1 mM EDTA, 50 µg/mL proteinase K] and incubate for 15 min at 55 degrees C. Inactivate proteinase K for 15 min at 80 degrees C and add 20 µL of deionized water. Centrifuge at 12,000 x g for 3 min. Transfer the supernatant to a new tube.

Concentration: Generally proteinase K is used in the concentration range of 50 to 500 µg/mL at 65 degrees C in the presence of SDS (0.5-1%).

Temperature optimum: 65 degrees C; 12X more active at 65 degrees C than at 25 degrees C.

pH: Proteinase K is stable over a wide pH range (4.0 to 12.5), with optimal activity at pH 6.5 to 9.5. It is most stable at pH 8.
Inactivation: Heat inactivate Proteinase K at 80 degrees C for 15 min. Phenol extraction is the recommended method to ensure complete inactivation.

Inhibited by: PMSF (0.1 to 1.0 mM of PMSF is usually sufficient for inhibition of Proteinase K)

Not inhibited by: Proteinase K is not inactivated by metal ions, chelating agents (e.g., EDTA), sulfhydryl reagents or by trypsin or chymotrypsin inhibitors. Activity can be stimulated by addition of denaturing agents (SDS and urea).

Citations & References (2)

Citations & References
Abstract
Improved cloning efficiency of polymerase chain reaction (PCR) products after proteinase K digestion.
Authors: Crowe J S; Cooper H J; Smith M A; Sims M J; Parker D; Gewert D;
Journal:Nucleic Acids Res
PubMed ID:2011503
Not available
Regulation of calreticulin expression during induction of differentiation in human myeloid cells. Evidence for remodeling of the endoplasmic reticulum.
Authors: Clark Robert A; Li Sen-Lin; Pearson Doran W; Leidal Kevin G; Clark Joshua R; Denning Gerene M; Reddick Robert; Krause Karl-Heinz; Valente Anthony J;
Journal:J Biol Chem
PubMed ID:12065601
Induction of differentiation of HL-60 human myeloid cells profoundly affected expression of calreticulin, a Ca(2+)-binding endoplasmic reticulum chaperone. Induction with Me(2)SO or retinoic acid reduced levels of calreticulin protein by approximately 60% within 4 days. Pulse-chase studies indicated that labeled calreticulin decayed at similar rates in differentiated and undifferentiated cells ... More
2 total citations

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