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XRN2

5'-3' exoribonuclease 2

Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription.

Gene Name: 5'-3' exoribonuclease 2
Synonyms: XRN2, 5'-3' exoribonuclease 2, 5-3 exoribonuclease 2, DHM1-like protein, DHP protein
Target Sequences: NM_012255 NP_036387.2 Q9H0D6

Publications (1)

1
Thrap3 promotes R-loop resolution via interaction with methylated DDX5. Hyun Je Kang #, Hye-Jin Eom #, Hongtae Kim, Kyungjae Myung , Hyug Moo Kwon, Jang Hyun Choi. Experimental & molecular medicine. 2021 Oct;;53:1602-1611. [Full Text Article] [PubMed:34697388] [PMC:PMC8569202] Related Antibodies: LS-B14272.

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Proteins (4)
Over-Expression Lysate (2)
Recombinant (2)
XRN2 (4)
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GST, N-terminus (1)
Myc-DDK (Flag) (3)
Human (3)
293T Cells (1)
HEK 293 Cells (2)
Wheat Germ Extract (1)
XRN2 Protein - 12.5% SDS-PAGE Stained with Coomassie Blue.
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Wheat Germ Extract
GST, N-terminus
2 µg/$439
XRN2 Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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293T Cells
Myc-DDK (Flag)
108.4 kDa
20 µg/$215
XRN2 Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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HEK 293 Cells
Myc-DDK (Flag)
108.4 kDa
100 µg/$710
XRN2 Protein - Purified recombinant protein XRN2 was analyzed by SDS-PAGE gel and Coomassie Blue Staining
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HEK 293 Cells
Myc-DDK (Flag)
108.4 kDa
20 µg/$1,107
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PLEASE NOTE

For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).