Required for DNA repair. Binds to DDB2 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 a component of numerous distinct DCX(DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2)(also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) 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. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8)(the CSA complex) plays a role in transcription-coupled repair(TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2.
Categories
Primary Antibodies
Clonality
monoclonal
Description
Required for DNA repair. Binds to DDB2 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 a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin- protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) 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. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2.
Host
Mouse
Immunogen
damage-specific DNA binding protein 1, 127kDa
Isotype
IgG2a
Molecular Weight
127 kDa
Reactivity
Human, Mouse, Rat
Regulatory
RUO
Synonyms
DDB p127 subunit, DDB1, DDBA, DNA damage binding protein 1, DNA damage binding protein a, HBV X associated protein 1, UV damaged DNA binding factor, UV DDB 1, UV
Uniprot
Q16531
Gene Id
1642
Clone No
3A0
Research Area
Epigenetics, Metabolism
Form
liquid
Format
liquid
Purification
Protein A+G purification
Purity
>=95% as determined by SDS-PAGE
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze / thaw cycles.)