RAD23B
| Gene Symbol | RAD23B |
|---|---|
| Entrez Gene | 5887 |
| Alt Symbol | HHR23B, HR23B, P58 |
| Species | Human |
| Gene Type | protein-coding |
| Description | RAD23 homolog B (S. cerevisiae) |
| Other Description | RAD23, yeast homolog of, B|UV excision repair protein RAD23 homolog B|XP-C repair complementing complex 58 kDa|XP-C repair complementing protein|XP-C repair-complementing complex 58 kDa protein |
| Swissprots | Q7Z5K8 B3KWK8 G5E9P0 P54727 Q8WUB0 |
| Accessions | AAN47194 EAW59016 EAW59017 P54727 AI285544 AI375313 AK125226 BAG54170 AK223479 BAD97199 AK293532 BAG57014 AK297986 BAH12700 AK316189 BAH14560 AL540969 AU125295 AW402384 AY313777 AAP81008 BC015805 BC020973 AAH20973 BE894394 BG678535 BI460482 BQ230600 BQ277025 BQ774932 CA866470 D21090 BAA04652 DC404422 DQ890563 ABM92180 DQ893726 ABM84652 NM_001244713 NP_001231642 NM_001244724 NP_001231653 NM_002874 NP_002865 |
| Function | The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn rec |
| Subcellular Location | Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S- phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin. |
| Top Pathways | Nucleotide excision repair, Protein processing in endoplasmic reticulum |
Rad23B CRISPR/Cas9 KO Plasmid (h) - sc-402106 from Santa Cruz Biotechnology
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Rad23B HDR Plasmid (h) - sc-402106-HDR from Santa Cruz Biotechnology
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Rad23B Double Nickase Plasmid (h) - sc-402106-NIC from Santa Cruz Biotechnology
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Rad23B Double Nickase Plasmid (h2) - sc-402106-NIC-2 from Santa Cruz Biotechnology
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Rad23B CRISPR Activation Plasmid (h) - sc-402106-ACT from Santa Cruz Biotechnology
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Rad23B CRISPR Activation Plasmid (h2) - sc-402106-ACT-2 from Santa Cruz Biotechnology
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Rad23B Lentiviral Activation Particles (h) - sc-402106-LAC from Santa Cruz Biotechnology
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Rad23B Lentiviral Activation Particles (h2) - sc-402106-LAC-2 from Santa Cruz Biotechnology
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Rad23B siRNA (h) - sc-60812 from Santa Cruz Biotechnology
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Rad23B shRNA Plasmid (h) - sc-60812-SH from Santa Cruz Biotechnology
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Rad23B shRNA (h) Lentiviral Particles - sc-60812-V from Santa Cruz Biotechnology
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hHR23b RNAi - H00005887-R01 from Novus Biologicals
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MISSION® esiRNA - EHU145881 from Sigma-Aldrich
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CompoZr® Knockout ZFN Kit - CKOZFN17896 from Sigma-Aldrich
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CompoZr® Knockout ZFN Kit, ZFN plasmid only - CKOZFND17896 from Sigma-Aldrich
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MISSION® 3′UTR Lenti GoClone™ - HUTR11561 from Sigma-Aldrich
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RAD23B siRNA (Human) - CRH3976 from Cohesion Biosciences
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RAD23B - MBS8224293 from MyBioSource
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shRNA set against Human RAD23 (NM_002874.4) - SHH388948 from Creative biogene
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Human RAD23B siRNA - orb264478 from Biorbyt
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RAD23B shRNA Plasmid (Human) - CHH3976 from Cohesion Biosciences
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