HUS1 Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, IHC-F, IF, ICC |
---|---|
Primary Accession | O60921 |
Reactivity | Rat, Pig, Bovine |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 31691 Da |
Gene ID | 3364 |
---|---|
Other Names | Checkpoint protein HUS1, hHUS1, HUS1 |
Dilution | Elisa=1:500-1000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ICC=1:100-500, |
Format | 0.01M TBS(pH7.4), 0.09% (W/V) sodium azide and 50% Glyce |
Storage | Store at -20 ℃ for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 ℃. |
Name | HUS1 |
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Function | Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:21659603). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a sliding clamp platform on DNA for several proteins involved in long- patch base excision repair (LP-BER) (PubMed:21659603). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:21659603). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). |
Cellular Location | Nucleus. Cytoplasm, cytosol. Note=In discrete nuclear foci upon DNA damage (PubMed:11077446). According to PubMed:11077446, localized also in the cytoplasm (PubMed:11077446). DNA damage induces its nuclear translocation (PubMed:11077446). Shuttles between the nucleus and the cytoplasm (PubMed:11077446). |
Tissue Location | Ubiquitous.. |
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