Alternative Name(s):

Ribonuclease H type II RNH1

Species: (Organism)

Homo sapiens (Human)

Gene Names:

RNASEH1

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED

Expression Region:

1-286aa

Subcellular Location:

Cytoplasm

Tissue Specificity:

Ubiquitous.

Protein Length:

Full Length

Pathway:

Mol. Weight:

37.6 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Epigenetics and Nuclear Signaling

Function:

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids

Involvement in disease:

Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 2 (PEOB2)

Relevance:

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

RNase H family

Reference:

"Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination." Skourti-Stathaki K., Proudfoot N.J., Gromak N. Mol. Cell 42:794-805(2011)