Recombinant full length protein corresponding to Human DDB2 aa 1-427.Sequence: MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDS DCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDS YRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFI KGIGAGGSITGLKFNPLNTNQFY
Conjugate
Unconjugated
Applications
Application Notes
IHC-P: 1/50 - 1/200; WB: 1/500 - 1/2000.
Target
Alternative Names
DDB2; damage-specific DNA binding protein 2, 48kDa; damage specific DNA binding protein 2 (48kD); DNA damage-binding protein 2; DDB p48 subunit; DDBB; FLJ34321; UV damaged DNA binding protein 2; UV DDB2; xeroderma pigmentosum group E protein; UV-DDB 2; UV
Required for DNA repair. Binds to DDB1 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as the substrate recognition module for the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA repair.
Pathway
Cul4-DDB1-DDB2 complex; DNA Repair; Direct p53 effectors; Dual incision reaction in GG-NER; Formation of incision complex in GG-NER; Global Genomic NER (GG-NER); Nucleotide Excision Repair
Citations
Publication ()
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