Summary
Specificity
Human, Mouse, Rat, Cattle, Pig, Horse, Dog, Chicken
Application
WB, IP, IF, ELISA, IHC-P
Basic Information
Immunogen
Amino acids 9-45 near the N-terminus of human DDB1.
Specificity
Human, Mouse, Rat, Cattle, Pig, Horse, Dog, Chicken
Clonality
Monoclonal Antibody
Application Notes
| Application | Note |
| WB | 1:100-1:1,000 |
| IP | 1-2 μg per 100-500 μg of total protein (1 mL of cell lysate) |
| IF(ICC) | 1:50-1:500 |
| ELISA | 1:100-1:1,000 |
| IHC-P | 1:50-1:500 |
Formulations & Storage [For reference only, actual COA shall prevail!]
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
Target
Function
Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:15448697, PubMed:14739464, PubMed:16260596, PubMed:16482215, PubMed:17079684, PubMed:16407242, PubMed:16407252, PubMed:16940174).
Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174).
The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174).
Also functions 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 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:28886238).
The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460).
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 (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899).
The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899).
DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621).
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 (PubMed:17041588).
DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143).
The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207).
DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity).
Biological Process
Biological process involved in interaction with symbiont Source: AgBase
Cellular response to DNA damage stimulus Source: UniProtKB
DNA damage response, detection of DNA damage Source: Reactome
DNA repair Source: GO_Central
Global genome nucleotide-excision repair Source: Reactome
Histone H2A monoubiquitination Source: UniProtKB
Nucleotide-excision repair Source: ProtInc
Nucleotide-excision repair, DNA damage recognition Source: Reactome
Nucleotide-excision repair, DNA duplex unwinding Source: Reactome
Nucleotide-excision repair, DNA incision Source: Reactome
Nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
Nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
Nucleotide-excision repair, preincision complex assembly Source: Reactome
Nucleotide-excision repair, preincision complex stabilization Source: Reactome
Positive regulation by virus of viral protein levels in host cell Source: AgBase
Positive regulation of gluconeogenesis Source: UniProtKB
Positive regulation of protein catabolic process Source: UniProtKB
Positive regulation of viral genome replication Source: AgBase
Positive regulation of viral release from host cell Source: AgBase
Post-translational protein modification Source: Reactome
Proteasomal protein catabolic process Source: MGI
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Regulation of mitotic cell cycle phase transition Source: UniProtKB
Rhythmic process Source: UniProtKB-KW
Transcription-coupled nucleotide-excision repair Source: Reactome
Ubiquitin-dependent protein catabolic process Source: UniProtKB
UV-damage excision repair Source: UniProtKB
Viral process Source: UniProtKB-KW
Cellular Location
Cytoplasm; Nucleus. Primarily cytoplasmic (PubMed:10777491, PubMed:11673459). Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459).
PTM
Phosphorylated by ABL1.
Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.
Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238). Deacetylation by SIRT7 impairs the interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238).
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