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Promega Corporation

Ribonuclease H

Ribonuclease H (RNase H) is an endonuclease that specifically hydrolyzes the phosphodiester bonds of RNA hybridized to DNA to produce 3´-OH and 5´-P-terminated products. It will not degrade single-stranded nucleic acids, double-stranded DNA or double-stranded RNA.

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Ribonuclease H

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Ribonuclease H

 Components

  • RNase H

    M428A1 x 50u
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  • Helix Freezer

This product is available through the Promega Helix onsite stocking program in a –20°C Helix Freezer. The program offers numerous convenient solutions to meet your lab's needs. Helix Freezers are available in two sizes: 5.7 cubic ft. or 9.7 cubic ft.


Click here to learn more about the Helix Collection »


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50u
0.5–2u/μl M4281 $ 197.00 Add to cart

Ribonuclease H

Close Window

Ribonuclease H

 Components

  • RNase H

    M428C1 x 250u
Close Window
  • This product can be added to a

  • Helix Freezer

This product is available through the Promega Helix onsite stocking program in a –20°C Helix Freezer. The program offers numerous convenient solutions to meet your lab's needs. Helix Freezers are available in two sizes: 5.7 cubic ft. or 9.7 cubic ft.


Click here to learn more about the Helix Collection »


Already a Helix Customer?

Request to add this product to your Helix »


250u
0.5–2u/μl M4285 $ 726.00 Add to cart


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QC Tests

Activity, DNase, RNase, endonuclease, cDNA synthesis.

Source

Recombinant E. coli strain.

Storage Buffer

20mM HEPES-KOH (pH 7.8 at 25°C), 1mM DTT, 50mM KCl, 50% (v/v) glycerol, 0.2mg/ml BSA.

Storage Conditions

Store at –20°C.

Unit Definition

One unit is defined as the amount of enzyme required to produce 1nmol of acid-soluble ribonucleotides from radiolabeled poly(rA):poly(dT) in 20 minutes at 37°C in 20mM HEPES-KOH (pH 7.8), 50mM KCl, 10mM MgCl2, 1mM DTT, 20μM radiolabeled poly(rA):poly(dT).

For product intended use please see Patents & Disclaimers tab.

Use Restrictions

M4281, M4285 For Laboratory Use. Outside of the United States, this product is intended for research use only unless otherwise stated.

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